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Protein interactions in Xenopus germ plasm RNP particles
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Nijjar, Sarbjit and Woodland, Hugh R. (2013) Protein interactions in Xenopus germ plasm RNP particles. PLoS ONE , Volume 8 (Number 11). Article number e80077. doi:10.1371/journal.pone.0080077 ISSN 1932-6203.
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Official URL: http://dx.doi.org/10.1371/journal.pone.0080077
Abstract
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. 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. 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.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QH Natural history > QH301 Biology | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Library of Congress Subject Headings (LCSH): | RNA-protein interactions, Ribosomes, Xenopus | ||||
Journal or Publication Title: | PLoS ONE | ||||
Publisher: | Public Library of Science | ||||
ISSN: | 1932-6203 | ||||
Official Date: | 12 November 2013 | ||||
Dates: |
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Volume: | Volume 8 | ||||
Number: | Number 11 | ||||
Page Range: | Article number e80077 | ||||
DOI: | 10.1371/journal.pone.0080077 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Open Access (Creative Commons) | ||||
Date of first compliant deposit: | 26 December 2015 | ||||
Date of first compliant Open Access: | 26 December 2015 | ||||
Funder: | Wellcome Trust (London, England) | ||||
Grant number: | WT084169 (WT) |
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