By a News Reporter-Staff News Editor at Gene Therapy Weekly -- Fresh data on Life Science Research are presented in a new report. According to news reporting from Coventry, United Kingdom, by NewsRx journalists, research stated, "Hermes is an RNA-binding protein that we have previously reported to be found in the ribonucleoprotein (RNP) particles of Xenopus germ plasm, where it is associated with various RNAs, including that encoding the germ line determinant Nanos1. To further define the composition of these RNPs, we performed a screen for Hermes-binding partners using the yeast two-hybrid system."
The news correspondents obtained a quote from the research from the University of Warwick, "We have identified and validated four proteins that interact with Hermes in germ plasm: two isoforms of Xvelo1 (a homologue of zebrafish Bucky ball) and Rbm24b and Rbm42b, both RNA-binding proteins containing the RRM motif. GFP-Xvelo fusion proteins and their endogenous counterparts, identified with antisera, were found to localize with Hermes in the germ plasm particles of large oocytes and eggs. Only the larger Xvelo isoform was naturally found in the Balbiani body of previtellogenic oocytes. Bimolecular fluorescence complementation (BiFC) experiments confirmed that Hermes and the Xvelo variants interact in germ plasm, as do Rbm24b and 42b. Depletion of the shorter Xvelo variant with antisense oligonucleotides caused a decrease in the size of germ plasm aggregates and loosening of associated mitochondria from these structures. This suggests that the short Xvelo variant, or less likely its RNA, has a role in organizing and maintaining the integrity of germ plasm in Xenopus oocytes. While GFP fusion proteins for Rbm24b and 42b did not localize into germ plasm as specifically as Hermes or Xvelo, BiFC analysis indicated that both interact with Hermes in germ plasm RNPs."
According to the news reporters, the research concluded: "They are very stable in the face of RNA depletion, but additive effects of combinations of antisense oligos suggest they may have a role in germ plasm structure and may influence the ability of Hermes protein to effectively enter RNP particles."
For more information on this research see: Protein interactions in Xenopus germ plasm RNP particles. Plos One, 2013;8(11):e80077. (Public Library of Science - www.plos.org; Plos One - www.plosone.org)
Our news journalists report that additional information may be obtained by contacting S. Nijjar, School of Life Sciences, University of Warwick, Coventry, Warwickshire, UK (see also Life Science Research).
Keywords for this news article include: Antisense Technology, Biotechnology, Europe, Coventry, Peptides, Proteins, Amino Acids, United Kingdom, Bioengineering, Life Science Research.
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