High impact information on yps

• One of these proteins was identified as the cold shock domain RNA-binding protein Ypsilon Schachtel (Yps), which we show binds directly to Exu and colocalizes with Exu in both the oocyte and nurse cells of the Drosophila egg chamber [1].
• As orb, yps and spn-E encode RNA-binding proteins, they may regulate the translation of unidentified RNAs necessary for the polarisation of the microtubule cytoskeleton [2].
• Furthermore, yps mutants partially suppress the premature cytoplasmic streaming of orb mutants [2].
• We show that yps interacts genetically with orb, a positive regulator of oskar mRNA localization and translation [3].
• We compare the functions of CncB to those of its vertebrate and invertebrate homologs, p45 NF-E2, Nrf and Skn-1 proteins, and suggest that the pharynx selector function of CncB is highly conserved on some branches of the evolutionary tree [4].

Biological context of yps

• In addition, there appears to be expression of yps mRNA in mesodermal tissue during embryogenesis [5].
• We predict that YPS would be an RNA-binding protein due to these results and the motifs which have been identified within the amino acid sequence [5].
• Subsequently, the cDNA for this gene was sequenced, and the identified open reading frame was named ypsilon schachtel (yps) [5].

Anatomical context of yps

• Ultrastructural analysis of Drosophila ovarian follicles differing in yolk polypeptide (yps) composition [6].
• The yolk protein genes (yps) of Drosophila melanogaster are only expressed in the ovary and fat body of female flies if they are supplied with proteinaceous food [7].

Analytical, diagnostic and therapeutic context of yps

• In situ hybridization shows that the yps mRNA is maternally loaded into the egg cytoplasm [5].
• The CSD of yps was purified and gel-shift analysis showed that this domain can interact with RNA [5].

References