|
|
|
Expr4504
|
MRG-1 is highly enriched in nuclei and concentrated on chromatin. In early embryos, MRG-1 is present in the nuclei of all blastomeres. In late embryos and young larvae, MRG-1 staining is higher in the nuclei of the two primordial germ cells, Z2 and Z3, than in somatic blastomeres. In larvae and adults, MRG-1 staining is seen primarily in the nuclei of germ cells, although it is also faintly visible in the nuclei of several somatic cell types, including intestinal cells. In the adult germ line, all germ nuclei in the mitotic and meiotic regions are stained. These results demonstrate that MRG-1 is present in the germ line at all stages of development and is maternally loaded into embryos. In addition, zygotically expressed MRG-1 is produced in all cells by at least the 100-cell stage; it accumulates to higher levels in the primordial germ cells than in somatic tissues. |
Expressed in nuclei. |
|
|
|
Expr15550
|
Both SLD-3 and SLD-2 showed asymmetric localisation, with more protein in the AB cell nucleus, than P1. This asymmetry was not limited to the MosSCI alleles, as we obtained a similar result using immuno-fluorescence of endogenous SLD-2. Asymmetric and asynchronous divisions continue beyond the two-cell stage, with the descendants of the AB cell (ABa and ABp) having shorter cell cycles than the descendants of the P1 cell (EMS and P2) with P2 having the longest S-phase of these cells. We analysed the abundance of SLD-2 and SLD-3 in 4-cell stage embryos and these two proteins remained asymmetric at this stage with EMS and P2 having significantly less protein than the AB cell lineage. SLD-2 abundance was also significantly lower in the P2 cell than the EMS cell. |
|
|
INX-3 detected during very early stages of development is likely to be maternally derived, since INX-3::GFP expressed zygotically is first detected by anti-GFP antibodies at approximately the 28-cell stage. |
|
Expr2546
|
At the late first larval (L1) stage, INX-3 is present transiently in some newly generated cells. The postembryonic motor neurons, descendants of the Pn.a cells, express INX-3 briefly. INX-3 is also detected briefly in cells of the first two divisions of the M blast cell, coelomocytes, and sex muscles. By the comma stage, corresponding to early embryonic morphogenesis, INX-3 is still broadly expressed, but the pattern of expression becomes more restricted as morphogenesis proceeds. Because INX-3 is localized principally in puncta at plasma membranes, it is hard to assign expression unambiguously to individual cells; however, expression in major cell types or organs is clear. Double-labeling embryos with anti-INX-3 and MH27, a mAb that binds AJM-1 in apical epithelial intercellular junctions, indicated that, at the comma stage, INX-3 is localized to the developing intestine, pharynx, and hypodermis (epidermis), at minimum. During late morphogenesis, from the 3-fold stage until hatching, INX-3 is found principally in the posterior pharynx (isthmus and terminal bulb), at the anteriormost tip of the pharynx, in the region of the posterior intestine (probably intestinal muscles or rectal cells) and in the hypodermis. Expression in these tissues continues throughout development into adulthood with the exception of the hypodermis. Hypodermal expression is strong at the time of hatching, and INX-3 is present in plaques at the intercellular boundaries between most hypodermal cells except at the ventral midline between paired P cells; however, INX-3 becomes undetectable in the hypodermis shortly after hatching. INX-3 protein is first detected at the embryonic 2-cell stage. It is localized to small plaques at cellcell interfaces and can be detected throughout early embryogenesis in a pattern suggesting that most or all cells express inx-3. In adults, INX-3 is reduced such that only a few plaques are associated with vulval muscles. In the late L3 stage, INX-3 expression begins in the sex myoblasts (SMs). Expression continues in SM descendants so that all 16 sex muscles stain with anti-INX-3 in early L4 animals, confirming results obtained with an inx-3::gfp translational fusion gene. |
At embryonic 2-cell stage, localized to small plaques at cellcell interfaces. At the late first larval (L1) stage, INX-3 is present transiently in some newly generated cells, and in cells of the first two divisions of the M blast cell, coelomocytes, and sex muscles. INX-3 is readily detectable in the cytoplasm of these cells, as well as in cell-surface plaques. By the comma stage, INX-3 is localized principally in puncta at plasma membranes. At comma stage, within intestinal cells, whose large size allows easy visualization of subcellular location, INX-3 is localized to the basal portion of lateral membranes. |
|
|
|
Expr14682
|
We first show the localization of UNC-59 at the cleavage furrow (previously shown with antibody staining, (Nguyen et al. 2000)) during a time lapse of cell divisions in early 2- to 4-cell stages of embryogenesis and throughout embryogenesis (cleavage rings in older embryos. Septins are also important for gonad morphogenesis and distal tip cell (DTC) migration (Nguyen et al. 2000) where UNC-59 protein is detected throughout gonad development in the rachis (previously shown with endogenously tagged unc-59::mKate, (Priti et al. 2018)) and DTCs. We highlight UNC-59/Septin localization in the DTC (previously shown with a transgene, (Finger et al. 2003)) at the L2 and L3 stages where it is organized into bundles (DeMay et al. 2011) and ring structures. The two bilateral sex myoblast cells express UNC-59 during their posterior to anterior migration in the L2 and early L3 stage and continue to express UNC-59 in these cells as they differentiate into vulval muscles in the late L3 to early L4 stages. Lastly, we show UNC-59/Septin expression and localization in tissue not previously reported: in the pharynx (cells of the buccal cavity, anterior procorpus, and terminal bulb); in the seam cells, both in bundles and at the cleavage furrows, beginning in the L1 stage and continuing throughout development and into the adult; and in sperm surrounding an embryo that has exited the spermatheca. |
|
|
CeE/Da = hlh-2 in the article. |
|
Expr1470
|
CeE/DA can first be detected in both nuclei of 2-cell embryos. Staining persists apparently in all nuclei of the early embryo for the first 150-200 minutes of development (100-200 cells). By 270 minutes of development (approx. 350 cells) a dramatic change in antibody staining has occurred in which persistent staining is seen in progressively fewer blastomeres. Most, but not all, blastomeres that initially retain CeE/DA antibody staining at this stage are neurons or their immediate precursors. There are a few neuronal precursors that are located away from the neuronal clusters in the embryo (for example the postembryonic neuroblast W), for which antibody staining was not detected. Therefore, although persistent antibody staining is largely restricted to neurons or their precursors, not every such cell is antibody-positive. CeE/DA-antibody staining is transient for the majority of these cells, with the staining progressively lost as differentiation and morphogenesis occur. This is most clearly evident at the 1.5-fold stage of embryogenesis, in which a lateral view of the embryo shows staining in the head, ventral nerve cord and tail. As the embryo begins elongating, the level of CeE/DA-antibody staining decreases in these cells. Note that most of these cells are postmitotic. Although the majority of cells lose CeE/DA-antibody staining during the later half of embryogenesis, a small percentage of cells remain antibody-positive through the remainder of embryogenesis and after hatching. There are 14 of these continually staining cells in the head and seven more in the tail region. Of the 14 head cells, 5 are pharyngeal. The pharyngeal nuclei have been identified, as two pharyngeal muscle nuclei (pm5L and R) and three pharyngeal gland cell nuclei (g1P, g2L and R). The remaining nine CeE/DA antibody-positive cells in the head are outside of the pharynx and are located in the neuronal cluster between the nerve ring and the posterior pharyngeal bulb. There are four bilateral pairs of stained nuclei and one positive nucleus lying along the ventral mid-line. Using hlh-2::GFP reporter strains and DiI staining, three of the bilateral pairs of neurons have been identified as ADL (L and R) and ASH (L and R) and RIC (L and R). The large number of neurons in this area makes it difficult to identify unambiguously each of the remaining three CeE/DA antibody-positive cells. The seven tail cells with nuclei that remain CeE/DA antibody-positive throughout embryonic development include the two Q neuroblasts and five cells were tentatively identified as DVA (an interneuron), the bilateral pair of intestinal muscle cells, the anal depressor muscle and the anal sphincter muscle. The two intestinal and two anal muscle cells are postmitotic and are non-striated muscles. CeE/Da is not detected in bodywall muscles. In addition to the 21 cells that are CeE/DA antibody-positive at hatching, there are several additional cells detected immunologically during subsequent development. One prominent set of cells that becomes CeE/DA antibody-positive during the L3 stage are the 16 developing vulval and uterine muscle cells (non-striated). These nuclei remain antibody-positive in the mature vulva, although staining intensity appears to decrease. Another prominent pair of postembryonic, CeE/DA antibody-positive nuclei are the distal tip cells (DTC). The DTC nuclei are CeE/DA antibody-positive from the start of gonad elongation in larval development and remain positive in adulthood. Very faint antibody staining can also be detected in the syncytial gonad. |
At all developmental stages, CeE/DA antibody staining is nuclear (except in the germline). |
|
early embryo (author) = blastula embryo (curator) --wjc. |
|
Expr1736
|
In early embryos, MES-3 protein is present in the nuclei of all cells. As embryogenesis progresses, staining gradually diminishes in somatic cells. In late embryos and L1 larvae, MES-3 is detectable in some somatic cells but is most prominent in Z2 and Z3, the primordial germ cells. The nuclear staining of MES-3 is reduced below detection in any of the four nonconditional alleles of mes-3. In wild type adults, MES-3 is most prominent in germline nuclei and is occasionally barely detectable in intestinal nuclei. In the germline, it is present at low levels in distal mitotic nuclei, undetectable in the pachytene region of the distal arm, and present at elevated levels in the proximal meiotic region and in oocytes. |
MES-3 is localized predominantly in nuclei. The immunolocalization pattern of MES-3 was analyzed in embryos, using confocal microscopy. Cells at different stages of mitosis were stained by affinity-purified anti-MES-3 antibody and anti-penta-acetylated H4 antibody to visualize chromosomes. During interphase and prometaphase, when condensed chromosomes are clearly visible in nuclei, MES-3 protein is not obviously concentrated on chromosomes; instead it appears evenly distributed in the nucleoplasm. During metaphase and early anaphase, when nuclear envelopes are broken down, some MES-3 protein is detectably associated with chromosomes. |
|
This information was extracted from published material (Archana Sharma-Oates, Andrew Mounsey and Ian A. Hope). |
|
Expr677
|
At one cell stage, there is no signal detected. Expression is first detected at two and four cell stage, pattern is variable at this stage. In most (35/48) of four cell embryos transcript is detected in posterior P1 cell or its immediate daughters. By 8 cell stage, signal detected in all blastomeres. In 3/48 expression is seen in the somatic AB cell and its immediate daughters, whereas 10/48 embryos ftt-2 messages were present in both lineages. ftt-2 transcript levels remain high in older embryos and during early elongation stage of morphogenesis, the transcript becomes localized to the region of the developing gonad and gut. Undetectable in maturing germ cells or maturing oocytes. |
|
|
|
|
Expr2579
|
SCC-1/COH-2 was expressed in germ cells throughout the development, including the adult stage. SCC-1/COH-2 was detected in virtually all mitotic germ nuclei. Similarly to somatic cells in embryos, SCC-1/COH-2 was dispersed in the cytoplasm at mitotic prometaphase and was absent from the condensed anaphase chromosomes in germ cells. In female germ cells that entered meiotic prophase in adult hermaphrodites, SCC-1/COH-2 was observed uniformly in the nuclei. It was unclear whether SCC-1/COH-2 localized to the condensed meiotic chromosomes, because of the strong SCC-1/COH-2 signal emitted from the nucleoplasm. SCC-1/COH-2 was detected also in male germ cells at mitosis and meiosis, but it was not detectable in mature sperm. SCC-1/COH-2 was strongly expressed in virtually all cells in early embryos, but its expression was gradually weakened, and the signal could hardly be detected in late embryos, in which cell division was ceased almost completely. Strong nuclear signals of SCC-1/COH-2 reappeared in larvae, though they were limited to a subset of cells. SCC-1/COH-2 was detectable only in cells that were going to divide. For example, in an L1 larva, intense SCC-1/COH-2 signals were detected in the 14 hypodermal V lineage cells, which divide synchronously. The SCC-1/COH-2 signal was dispersed and not detectable on condensed chromosomes, as observed in embryos of an intermediate stage. In a slightly older L1 larva, expression of SCC-1/COH-2 was seen in 22 P lineage cells to constitute the ventral nerve cord and in four Q lineage cells to produce posterior neuronal cells, all of which divide at the same time. In this L1 larva, no signal was detected in the V lineage cells, suggesting that the SCC-1/COH-2 protein is present only for a short time in the cell cycle, and likely to be degraded quickly after cell division. Larvae of later stages also expressed SCC-1/COH-2 in dividing cells: in an L3 larva, SCC-1/COH-2 was detected in four M lineage cells to produce the uterine and vulval muscle cells and in 10 P lineage vulval precursor cells, which divide concurrently. The embryos were stained with both anti-SCC-1/COH-2 antibodies and an antibody against a component of the nuclear pore complexes. The SCC-1/COH-2 signal was evenly distributed within the nuclear envelope except for the chromosomal region, suggesting that SCC-1/COH-2 molecules dissociated from the chromosomes at metaphase were trapped by the nuclear envelope. Consistently with this interpretation, the SCC-1/COH-2 staining around the metaphase plate was no longer seen at later stages of embryogenesis involving >30 cells, where nuclear envelope is known to break down before metaphase. SCC-1/COH-2 was dispersed into the whole cytoplasm of metaphase cells at these stages. |
SCC-1/COH-2 seemed to localize to the chromosomes in a cell cycle-dependent manner. In interphase, SCC-1/COH-2 was seen throughout the nucleus, overlapping largely with DNA. At mitotic prophase, SCC-1/COH-2 started to separate from condensing chromosomes, and it was not detected on the chromosomes at prometaphase and metaphase. At metaphase, the SCC-1/COH-2 signal seemed as if surrounding the metaphase plate, although it was possible that a small amount of SCC-1/COH-2 was remaining on the metaphase chromosomes but escaped detection, because cohesin is reported to become detectable on metaphase chromosomes only after detergent extraction of soluble background in other metazoans. The SCC-1/COH-2 signal was then dispersed in the cytoplasm at anaphase. At telophase, the SCC-1/COH-2 protein began to reaccumulate on the chromosomes. |
|
Picture: Fig. 5. The same pattern was seen with two separate antibodies raised against distinct PLP-1 peptides, and both nuclear and P granule expression was largely eliminated in plp-1 (RNAi) embryos, confirming their specificity. |
|
Expr8706
|
Immunoreactive PLP-1 localizes to the nuclei of all blastomeres beginning by the two-cell stage of embryogenesis, implying that PLP-1 is a maternally encoded transcription factor. It is also present in the germline-specific P granules of early embryos. |
PLP-1 is transiently asymmetrically localized during telophase of the dividing EMS cell (observed in 12 embryos at the correct stage), with higher levels of the protein in the chromatin of the future E cell nucleus and low or undetectable levels in that of MS. A similar transient asymmetry in PLP-1 levels was observed at many divisions throughout early development, starting at cleavage of the zygote, with higher levels seen in the cytoplasm and forming nucleus of the posterior daughter, P1 (observed in 5 embryos). The anteroposterior asymmetry in PLP-1 was also observed in the AB lineage during the division of the AB granddaughters (observed in 7 embryos): for example, PLP-1 is higher in the chromatin of the posterior daughter ABalp than that of its anterior sister ABala. In all cases, the asymmetry was observed only during telophase and at the time that nuclei were reassembling after cell division; the staining was symmetric at all other times. PLP-1 was always seen at higher levels in the forming nuclei of the posterior daughters. |
|
early embryo(author) = blastula embryo(curator). |
|
Expr584
|
gld-1 mRNA is contained in all blastmeres of embryos with 8 or fewer cells. Subsequently, gld-1 mRNA disappears rapidly from somatic blastmeres and is only detected in the germ lineage. By the 16 cell stage, gld-1 mRNA is only detected in P3. |
|
|
|
|
Expr2551
|
In situ hybridization analysis revealed that spn-4 mRNA was abundant in early embryos. The mRNA was present at the same level in all blastomeres up to the 4-cell stage. Afterwards, it persists in the P blastomere and its sister, and then just the germ lineage. The mRNA was also present in the adult gonads. |
|
|
|
|
Expr2947
|
In late embryos (after the comma stage) matefin staining decreased in all somatic cells but intensified in the nuclear envelopes of the two primordial germ cells, Z2 and Z3. The identity of Z2 and Z3 cells was verified by double labeling with antibodies against PGL-1, which is specific to germ cells. Throughout larva stages L1-L4 and in adults, matefin was present only in germ cells. Matefin signal declined during spermatogenesis and was undetectable in sperm. |
Matefin was detected at the nuclear envelope of all early embryonic cells. |
|
early embryo(author) = blastula embryo(curator). |
|
Expr572
|
SKN-1 protein first becomes visible in oocyte and sperm pronuclei before the first mitotic division of the zygote. SKN-1 becomes cytoplasmic as AB and P1 enter mitosis. P2 and EMS have more SKN-1 than AB daughters. By the 8-cell stage, the granddaughters of AB do not stain for SKN-1, but P1 granddaughters do. SKN-1 is not detectable by the 12-cell stage. |
After the first cleavage, SKN-1 protein locates at the nuclei of AB and P1. As AB and P1 enter mitosis, SKN-1 protein is distributed throughout cytoplasm. |
|
Maternal effect. early embryo(author) = blastula + gastrulating embryo(curator). |
|
Expr576
|
In adult hermaphrodites, mex-1 mRNA is detected in the syncytial core of the gonad and in oocytes at all stages of maturation. In 1 and 2-cell stage embryos, mex-1 mRNA is distributed uniformly, but then appears to be degraded rapidly in somatic blastomeres but remains in germ line blastomeres in subsequent divisions. After P4 divides, mex-1 mRNA is not detected. |
|
|
This information was extracted from published material (Archana Sharma-Oates, Andrew Mounsey and Ian A. Hope). |
|
Expr706
|
NHR-2 is detected in the nuclei of embryos as early as 2-cell stage. The protein is present in every nucleus until the 16-20 cell stage then no longer detected in germline precursor P4 and its sister D but at this point expression in other cells increase. No staining during or just after mitosis. 28-cell stage: Staining in E and MS descendants, variable expression generally weak particularly in E cells. Staining in ABplp and ABpr descendants also variable but can be quite strong. The other 10 AB cells and 4 C cells exhibit reproducible strong expression. 51-cell stage: No expression in descendants of E. Staining in C cells, many AB cells and some MS cells (particularly those in anterior and dorsal positions). As embryogenesis progresses NHR-2 expression is restricted to anterior and dorsal regions of embryo. 250 cell stage: Nuclei staining include (but not limited to) Cp descendants contributing to hyp7 synctium, many but not all AB descendants. NHR-2 last detected in one or a few nuclei in vicinity of excretory cell before expression ceases at early comma stage. |
|
|
See Expression pattern 546 for distribution of APX-1 protein. early embryo(author) = blastula embryo(curator). |
|
Expr545
|
Between the newly-fertilized 1-cell stage and the 8-cell stage, apx-1 mRNA is present in all blastomeres at equivalent levels. After the 8-cell stage, apx-1 mRNA rapidly disappears from somatic blastomeres; in 12-cell stage embryos, apx-1 mRNA is visible in the P3 blastomere, but disappears from MS and all other blastomeres. In the 36-cell stage and later embryos, apx-1 mRNA was detected in one to five unidentified nuclei. |
|
|
|
|
Expr2575
|
In situ hybridization analysis revealed that spn-4 mRNA was abundant in early embryos. The mRNA was present at the same level in all blastomeres up to the 4-cell stage. Afterwards, it persists in the P blastomere and its sister, and then just the germ lineage. The mRNA was also present in the adult gonads. |
|
|
|
|
Expr15824
|
MIP-1 is omnipresent throughout development, localizing exclusively to the germline precursor lineage (from P0 through P4) and remaining prominent in the germline pro- genitor cells Z2 and Z3. In contrast, MIP-2 begins to dissipate in P3 and is virtually undetectable when Z2 and Z3 are born. |
|
|
|
|
Expr13800
|
GFP::WAGO-4 was exclusively expressed in the germline and all oocyte cells in gravid adults in hermaphrodites but not significantly expressed in the male germline. In early embryos, WAGO-4 is expressed in the P1 and EMS cells. In late embryos, WAGO-4 was exclusively expressed in Z2/Z3 cells. Interestingly, we observed that WAGO-4 accumulated at some distinct perinuclear foci. |
|
|
|
|
Expr15143
|
WAGO-4 is a germline-expressed protein that segregates with the P lineage blas- tomeres and localizes to perinuclear foci. GFP::ZNFX-1 and GFP::WAGO-4 colocalized with PGL-1::TagRFP in P1-P3 germline blastomeres, suggesting that ZNFX-1 and WAGO-4 are P granule factors. |
|
|
|
|
Expr15142
|
We observed GFP::ZNFX-1 expression in the adult germline as well as in developing germ cells during all stages of embryonic and larval development. No GFP::ZNFX-1 expression was observed in somatic tissues. After fertilization, C. elegans zygotes undergo a series of asymmetric cell divisions in which germline determinants segregate with germline blastomeres. During embryonic development, ZNFX-1 foci were concentrated in, and segregated with, the germline blastomeres. In adult germ cells, GFP::ZNFX-1 was concentrated in foci that were distributed in a perinuclear pattern around nuclei. We conclude that znfx-1 encodes a germline-expressed protein that segregates with the germline and localizes to perinuclear foci in adult germ cells.GFP::ZNFX-1 and GFP::WAGO-4 colocalized with PGL-1::TagRFP in P1-P3 germline blastomeres, suggesting that ZNFX-1 and WAGO-4 are P granule factors. |
|
|
early embryo(author) = blastula embryo(curator). |
|
Expr574
|
PIE-1 protein is localized to the posterior of the zygote and continues to be observed in the germ line P1 through P4 and Z2 and Z3, but not in somatic blastomeres. |
PIE-1 is associated with P granules in germline blastomere cytoplasm. At mitosis, PIE-1 accumulates around the centrosomes of the spindle and PIE-1 decreases in the cytoplasm. PIE-1 staining remains only in the germline blastomeres after division. After P4 divides, PIE-1 persists in both Z2 and Z3 centrosomes. |
|
early embryo(author) = blastula embryo(curator). |
|
Expr575
|
In oocytes,1-cell and 2-cell stage embryos, pie-1 mRNA is distributed uniformly. After the 4-cell stage, pie-1 mRNA was lost from somatic blastomeres and remained in the germ lineage. PIE-1 protein was first detected in maturing oocytes, where it is uniformly distributed. PIE-1 level increase during the one cell stage. PIE-1 protein also exists in P1, P2 P3, P4, Z2 and Z3. In P4, PIE-1 is found equally in the P4 daughters (Z2 and Z3) in contrast to earlier divisions in which PIE-1 is localized to the posterior cytoplasm and posterior centrosomes during mitosis. |
A subset of PIE-1 molecules are associated with P granules, but there is a diffuse cytoplasmic component of PIE-1 staining in contrast to the punctate P granule pattern. PIE-1 protein is cytoplasmic until the 2-cell stage, after which it is increasingly nuclear. PIE-1 protein distribution in P0, P1, P2 and P3 follows a similar pattern: initially uniform cytoplasmic distribution, followed by asymmetric cytoplasmic localization at the time of P granule migration, and asymmetric cytoplasmic and centralsomal localizations during mitosis. |
|
early embryo(author) = blastula + gastrulating embryo(curator). |
|
Expr578
|
Antibody staining is first detected at the bend of the reflexed hermaphrodite gonad. PAR-1 is seen in newly formed, but not mature oocytes nor newly fertilized zygotes. PAR-1 reappears in the late zygote, when both pronuclei are decondensed and the female pronucleus is just starting to migrate toward the posterior. In P0 through P3, it is localized in the posterior periphery so that it is distributed to the germ line blastomeres. When P4 divides, PAR-1 is distributed evenly and distributed to both Z2 and Z3. After P4 divides, PAR-1 gradually fades until it disappears at morphogenesis. |
PAR-1 is membrane-associated. In dividing cells, it is restricted to the posterior until P4 divides, at which time it is located throughout the periphery. PAR-1 co-localizes with P granules. |
|
Antibodies against the amino and carboxy termini gave the same results. early embryo(author) = blastula + gastrulating embryo(curator). |
|
Expr579
|
PAR-1 is found in the cortex of germ line cells in the whole adult gonad. In early embryos, cortical PAR-2 expression continues in P0, P1, P2, P3 and P4 (the cells of germline lineage), fades in Z2 and Z3. In all but P4, PAR-1 exhibits an asymmetric distribution. |
In the distal gonad, PAR-2 staining is strongest at septa between nuclei. In the proximal gonad, PAR-2 is found uniformly in the periphery. PAR-2 is associated with the cortical cytoskeleton. PAR-2 becomes localized to the posterior cortex in P0 through P3. During the symmetrical division of P4, PAR-2 is uniformly distributed at the cortex so that both Z2 and Z3 initially show PAR-2. |
|
|
|
Expr12428
|
NEG-1::GFP is asymmetrically localized in the early embryo. NEG-1::GFP was detected in the zygotic nucleus and at equal levels in both nuclei of the two-cell embryo (23 of 23). However, at the four-cell stage, NEG-1::GFP expression was markedly higher in nuclei of the anterior AB blastomeres than in the nuclei of EMS and P2 (31 of 34). Following the four-cell stage, NEG-1::GFP remained high in the granddaughters of the AB blastomere and diminished progressively in subsequent divisions (data not shown). In the adult germline, NEG- 1::GFP was observed in the nuclei of distal germ cells and the nuclei of growing oocytes except for the most proximal oocyte. Moreover, intense sub-nuclear localization of NEG-1:GFP was observed on condensed chromatin. |
|
|
Staining with anti-NOS-3 antibodies was specific, in that it was dramatically reduced in nos-3 deletion mutants. |
|
Expr1203
|
NOS-3 protein detected throughout the germ-line tissue during larval development. In addition to staining in the larval gonad, NOS-3 expression was also observed in embryos. Specifically, NOS-3 was found in P1P4, and later in germ-line progenitor cells, Z2 and Z3. |
At all stages of germ-line development, NOS-3 was predominantly cytoplasmic: this was evidenced by the dark, non-staining `holes' corresponding to nuclei in the germ line at the larval L3 stage. The distribution of NOS-3 overlapped with regions of the cytoplasm containing P granules, detected using anti-PGL-1 antibodies; however, within the cytoplasm, NOS-3 staining was uniform and diffuse throughout. At the late L4 stage, NOS-3 was detected in germ cells in mitosis and meiotic pachytene, but decreased in the spermatogenic region. Although the distribution of NOS-3 in P cells was punctate, it did not precisely coincide with P granules. |
|
Removing the coding region, and using only the Bluescript vector as a probe, does not show staining except a little background. As a negative control, the dpy-20 probe was used for RNA in situ hybridization and no staining in embryos was detected. |
|
Expr1099
|
1-cell, 2-cell and 4-cell embryos show uniform expression pattern. Expression in later embryos and young larvae is predominant in the head region. |
|
|
|
|
Expr15548
|
Both SLD-3 and SLD-2 showed asymmetric localisation, with more protein in the AB cell nucleus, than P1. This asymmetry was not limited to the MosSCI alleles, as we obtained a similar result using immuno-fluorescence of endogenous SLD-2. Asymmetric and asynchronous divisions continue beyond the two-cell stage, with the descendants of the AB cell (ABa and ABp) having shorter cell cycles than the descendants of the P1 cell (EMS and P2) with P2 having the longest S-phase of these cells. We analysed the abundance of SLD-2 and SLD-3 in 4-cell stage embryos and these two proteins remained asymmetric at this stage with EMS and P2 having significantly less protein than the AB cell lineage. SLD-2 abundance was also significantly lower in the P2 cell than the EMS cell. |
|
|
|
|
Expr15549
|
Both SLD-3 and SLD-2 showed asymmetric localisation, with more protein in the AB cell nucleus, than P1. This asymmetry was not limited to the MosSCI alleles, as we obtained a similar result using immuno-fluorescence of endogenous SLD-2. Asymmetric and asynchronous divisions continue beyond the two-cell stage, with the descendants of the AB cell (ABa and ABp) having shorter cell cycles than the descendants of the P1 cell (EMS and P2) with P2 having the longest S-phase of these cells. We analysed the abundance of SLD-2 and SLD-3 in 4-cell stage embryos and these two proteins remained asymmetric at this stage with EMS and P2 having significantly less protein than the AB cell lineage. SLD-2 abundance was also significantly lower in the P2 cell than the EMS cell. |
|
