cgt, courgette, BG:DS00929.14
maternal - a DEAD-box RNA helicase - interacts with eIF5B and promotes translation of and mRNAs - overcomes the repressive effect of Nanos translational control element - functions in piRNA biogenesis as a component of an Amplifier complex - Maternally-expressed Vas is required for oogenesis, transposon silencing in the female germ line, anterior-posterior embryonic patterning, and germ cell specification.
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 6.05
Genes with CDS overlap: vas and solo share promoter, first exon and N-terminal coding sequences (137 residues).
Interacts with eIF5B and faf. Interacts with gus (via B30.2/SPRY domain) and Fsn (via B30.2/SPRY domain). Interacts with aub, me31B, eIF-4a and TER94. Interacts with piwi; this interaction is RNA independent. Interacts with Dcr-1 and Fmr1; these interactions occur in the polar granules.
Ubiquitinated during oogenesis. Deubiquitinated by faf, which protects this protein from proteasome-mediated degradation.
The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\vas using the Feature Mapper tool.
syncitial blastoderm, but is degraded upon cellularization, including in the
germ cells. It is zygotically expressed in the germ cells at stage 11, and can be seen in the embryonic gonad at stage 13-14.
The vas protein is expressed in germ cells at the larva/pupa transition, 108 hrs AEL.
In stage 10 oocytes, vas protein, osk protein, and stau protein colocalize at the posterior pole. In early embryos, vas protein and osk protein localize to the polar granules but stau protein does not colocalize with them. It is present in a thin crescent apposed closely to the posterior cortex and disappears before the pole cell stage. A GFP-Vas fusion protein was used to determine the vas protein distribution.
vas protein is concentrated in the form of polar granules at the posterior pole in early embryos. A low level of staining is also seen throughout the embryo during cleavage stages. vas protein is also present in egg chambers. Protein expression in mutants of vas, stau, osk, tud, vls, and BicD were studied.
vasa protein is detected in larval and pupal ovaries in the oogonial cells and their precursors. It is abundant in the germaria of adult ovaries and is also abundant in the pronurse cell nuclei in early stages of oogenesis. vasa protein is transported to the oocyte starting in stage 8 and is concentrated at the posterior pole, although it is detectable at lower levels throughout the oocyte. vasa protein is also detected in males in the larval spermatogonial cells and in cyst cells of the adult testis. In early cleavage stage embryos, a shallow posterior-anterior gradient of vas protein is seen with the highest concentration at the posterior pole. Later the pole cells stain heavily and the pole cell and subsequent gonadal expression persists throughout embryogenesis. In ovaries lacking tud, vls, nos, and pum, vas protein localizes to the posterior pole of the oocyte normally but in ovaries lacking osk and stau, vas protein fails to distribute asymmetrically. BicC mutations affect vas protein distribution while BicD mutations do not. capu and spir abolish localization of vas protein to pole cells. vas protein is detected in ovaries of egl, mus301, qua, Bic-F, mr, Fs(2)Y12, and vss mutant females.
vas protein is located at the posterior pole of early embryos. This posterior localization is abolished in mutants of stau, vas, spir, capu, and osk. Posterior localization of vas protein is less striking in tud and vls mutants than in wild type embryos and indistinguishable from wild type in nos and pum mutants.
vas protein in both late-stage oocytes and in early embryos is localized to the posterior pole, and thus differs from the uniform distribution of vas transcript at the same stage. In addition to late-stage oocytes, the vas protein is found in germline stem cells and nurse cells of ovaries. In adult males, the vas protein is present in male germline stem cells during early spermatogenesis.
GBrowse - Visual display of RNA-Seq signalsView Dmel\vas in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for identity of: vas CG3506
Source for merge of: vas CG46283
Annotation CG43081 split into CG46282 (corresponds to solo) and CG46283 (corresponds to vas) in release 6.06 of the genome annotation. Split supported by distinct sequences and functions of vas and solo proteins.
Annotations CG3506 and CG33678 merged as CG43081 in release 5.31 of the genome annotation.
vas is required for the establishment of both anterior-posterior and dorsal-ventral polarity of the oocyte.
Molecular analysis of vas alleles suggests that recruitment of vas to the pole plasm must depend on protein-protein interactions, but, once localized, vas must bind to RNA to mediate germ cell formation.
The vas gene is critical for normal and ectopic localization of the posterior signal.
vas mutants exhibit deletion of the abdomen and pole plasm; amorphic mutants are sterile.
Mutation in vas results in a maternal effect "grandchildless knirps-like" phenotype.