The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling

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dc.contributor.authorFrehlick, Lindsay J
dc.contributor.authorEirín-López, José María
dc.contributor.authorJeffery, Erin D
dc.contributor.authorHunt, Donald F
dc.contributor.authorAusió, Juan
dc.date.accessioned2014-08-18T21:56:38Z
dc.date.available2014-08-18T21:56:38Z
dc.date.copyright2006en_US
dc.date.issued2006-04-28
dc.descriptionBioMed Centralen_US
dc.description.abstractBackground: Nucleoplasmin is a nuclear chaperone protein that has been shown to participate in the remodeling of sperm chromatin immediately after fertilization by displacing highly specialized sperm nuclear basic proteins (SNBPs), such as protamine (P type) and protamine-like (PL type) proteins, from the sperm chromatin and by the transfer of histone H2A-H2B. The presence of SNBPs of the histone type (H type) in some organisms (very similar to the histones found in somatic tissues) raises uncertainty about the need for a nucleoplasmin-mediated removal process in such cases and poses a very interesting question regarding the appearance and further differentiation of the sperm chromatin remodeling function of nucleoplasmin and the implicit relationship with SNBP diversity The amphibians represent an unique opportunity to address this issue as they contain genera with SNBPs representative of each of the three main types: Rana (H type); Xenopus (PL type) and Bufo (P type). Results: In this work, the presence of nucleoplasmin in oocyte extracts from these three organisms has been assessed using Western Blotting. We have used mass spectrometry and cloning techniques to characterize the full-length cDNA sequences of Rana catesbeiana and Bufo marinus nucleoplasmin. Northern dot blot analysis shows that nucleoplasmin is mainly transcribed in the egg of the former species. Phylogenetic analysis of nucleoplasmin family members from various metazoans suggests that amphibian nucleoplasmins group closely with mammalian NPM2 proteins. Conclusion: We have shown that these organisms, in striking contrast to their SNBPs, all contain nucleoplasmins with very similar primary structures. This result has important implications as it suggests that nucleoplasmin's role in chromatin assembly during early zygote development could have been complemented by the acquisition of a new function of non-specifically removing SNBPs in sperm chromatin remodeling. This acquired function would have been strongly determined by the constraints imposed by the appearance and differentiation of SNBPs in the sperm.en_US
dc.description.reviewstatusRevieweden_US
dc.description.scholarlevelFacultyen_US
dc.description.sponsorshipThis work was supported by grants from Natural Sciences and Engineering Research Council of Canada (NSERC), Grant number OGP0046399 (to J.A.), by a Postdoctoral Marie Curie International Fellowshipwithin the 6th European Community Framework Programme (to J.M.E.-L)and by an NSERC postgraduate scholarship (to L.J.F.)en_US
dc.identifier.citationFrehlick et al. The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling. BMC Genomics 2006, 7 :99en_US
dc.identifier.urihttp://www.biomedcentral.com/1471-2164/7/99
dc.identifier.urihttp://dx.doi.org/10.1186/1471-2164-7-99
dc.identifier.urihttp://hdl.handle.net/1828/5574
dc.language.isoenen_US
dc.publisherBioMed Centralen_US
dc.subject.departmentDepartment of Biochemistry and Microbiology
dc.titleThe characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodelingen_US
dc.typeArticleen_US

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