ovarette, pkl, pumuckel, bem, ovt
novel posterior group gene - posttranscriptional repressor - binds and regulates mRNA - Nanos acts as a molecular clamp that modulates the RNA-binding and repression activities of Pumilio
Stage-specific extension of 3' UTRs observed during embryogenesis (FBrf0215804); all variants may not be annotated.
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.46
A non-AUG start codon may be used for translation of one or more transcripts of this gene; based on the presence of conserved protein signatures within the 5' UTR without an in-frame AUG (FBrf0243886).
The doublet of 156 kD pum proteins observed in Western blots may be generated by posttranslational modification.
It is not known how the 130 kD pum isoform is generated; it may be generated by an alternate transcript, or by post-translational modification of the 156 kD isoform. Antibodies generated against exons 4, exons 4-13 and exons 11-13 of the 156 kD pum isoform cross-react with the 130 kD isoform.
RNA-protein and protein-protein interaction assays indicate that nos protein forms a ternary complex with the RNA-binding domain of pum protein and the NREs (nanos response element) in the 3'' UTR of maternal hb mRNA.
The carboxy-terminus of the protein contains eight repeated units which are strikingly similar to a region of eight repeats in the S. cerevisiae YGL023 gene.
Interacts with nos and brat. Acts via the formation of a quaternary complex composed of pum, nos, brat and the 3'-UTR mRNA of hb.
The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. RNA-binding occurs on the concave side of the surface. Pum is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\pum using the Feature Mapper tool.
pum protein is detected in a broad pattern in the CNS with enriched expression in the calyx of the mushroom body.
pum protein is detected in germarium region 1, with highest levels in germline stem cells, and lower levels in in dividing cystoblasts.
Comment: single neuron
Comment: 1 or 2 neurons
GBrowse - Visual display of RNA-Seq signalsView Dmel\pum 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: pum CG9755
The "bem1" mutation may be an allele of pum; pum13 fails to complement bem1 female sterility, bem1 female fertility is partially rescued by ovary specific expression of pum and one of three pum transcripts is absent from bem1 heads.
Source for merge of pum anon-WO0172774.19 was sequence comparison ( date:051113 ).
Affinity binding in extracts from adult ovaries reveals that 1090 genes are consistently associated with pum with a false discovery rate of <1%. Analysis on embryos identifies 165 genes that are associated with pum. The overlap between the two groups contains 31 genes.
pum is an important regulator of synaptic growth and plasticity at the neuromuscular junction.
nos and pum control the elaboration of high-order dendritic branches of class III and IV, but not class I and II, dendritic arborization neurons. nos and pum require each other to control dendrite morphogenesis, but hb is not required.
pum plays multiple roles in germline development, gonadogenesis, oogenesis and embryogenesis.
Maternally deposited nos is essential for germ cell migration. Lack of zygotic activity of nos and pum has a dramatic effect on germline development of homozygous females. nos and pum act in the germline, affecting germline stem cell development. nos function lies in the differentiation of the stem cell progeny, the cystoblast. nos and pum may interact with different partners in the germline.
pum mutant ovaries fail to maintain stem cells and all germline cells differentiate into egg chambers.
'ovarette' mutations of pum affect the assymetric division of germline stem cells.
Isolated during a screen for mutations that disrupt Bolwig's organ or Bolwig's nerve development.
A study of the mechanisms of nos-mediated translational repression indicates that nos and pum determine posterior morphology by promoting the deadenylation of maternal hb mRNA, thereby repressing its translation.
The pum RNA-binding domain is an evolutionarily conserved, 334 amino acid region at the carboxy terminus of the protein.
Nurse cell-specific genes are functional in the pseudonurse cells of otu mutants, but the transport of pum, otu, ovo and bcd RNAs to the cytoplasm is affected. The nuclear localisation of otu and pum mRNA correlates with chromosome polytenisation.
nos response elements (NRE) in the hb mRNA mediate nos repression of hb maternal transcript translation. pum protein is an NRE binding factor, pum recognises the NRE and recruits nos, the resulting complex is thought to inhibit some component of the translation machinery.
Mutation in pum increases neuronal excitability, possibly as a result of a defect in an ion channel structural or regulatory gene.
Flies defective in pum display uncoordination, inability to fly and greatly reduced fertility. Mutant larvae display a more rapid onset of a phenomenon called long term facilitation so causes increased neuronal excitability.
The pum gene product recognises and binds directly to the nanos response elements (NREs) in the 3' region of hb. The nos gene product then binds to pum and this complex interferes with translation of hb mRNA.
The pumilio gene is expressed maternally. pumilio RNA is enriched at the posterior pole of the egg, but is not required for either the expression of nanos protein or its transport to the presumptive abdomen. Amorphic alleles show that the function of pumilio is absolutely required for abdomen formation.
pum gene product affects the asymmetric division of the female germline stem cell (GSC).
Cloning, molecular characterization and analysis of pum mRNA and protein expression reveals that pum does not act in a spatially restricted fashion.
pum is critical for pole plasm formation but not required for the initial localization or synthesis of the posterior signal. The abdominal phenotype of pum embryos can be partially rescued by cytoplasmic transplantation of wild type posterior pole plasm into the abdominal region. The signal required for abdominal segmentation is present in the pole plasm from pum embryos but cannot reach the abdominal region.
Mutations in maternal posterior class gene pum do not interact with RpII140wimp.
Mature follicles are immunologically stained for asymmetric distribution of ecdysteroid-related antigen. During late oogenesis localisation of the antigen changes dramatically suggesting the antigen plays a role in early embryogenesis and, perhaps, in pattern formation.
pum gene function is not required for pole cell formation.
pum plays a role in polar granule formation.
Transplantation experiments suggest that pum is involved in the transport of a signal required in the abdomen from the pole plasm to the abdominal region.
Wild-type allele of pum involved in development of the abdomen (embryos) and of the imaginal discs (larvae or pupae), perhaps having a function in signal transport. Embryos derived from pum/pum females (strong allele) form two instead of eight abdominal segments; head, thorax and telson are normal. Pole cells are formed by the pum embryos and these cells function normally when transplanted into otherwise sterile embryos. There is no paternal rescue. Partial rescue of the pum abdominal phenotype (at the site of the injection) can be obtained with cytoplasm from the posterior pole of (1) wild-type embryos or (2) pum embryos. When pum is combined with tsl (mutant in which the abdominal region is placed next to the pole plasm), a rescue of abdominal segments may occur. pum opposite a deficiency or another pum allele results in a recessive zygotic visible phenotype; pum adult flies have additional postalar, dorsocentral and scutellar bristles and reduced viability. Most mutant alleles are semi-lethal and have abnormal bristles when homozygous.