title: The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling.
abstract: BACKGROUND
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Department of Biochemistry and Microbiology, University of Victoria, Petch Building, Victoria, BC, V8W 3P6, Canada. ljb@uvic.ca
authors.forename: Lindsay J
authors.initials: LJ
authors.lastname: Frehlick
authors.forename: José María
authors.initials: JM
authors.lastname: Eirín-López
authors.forename: Erin D
authors.initials: ED
authors.lastname: Jeffery
authors.forename: Donald F
authors.initials: DF
authors.lastname: Hunt
authors.forename: Juan
authors.initials: J
authors.lastname: Ausió
mesh_terms: D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002025:Bufonidae; D002843:Chromatin / Q000737:chemistry* / Q000378:metabolism; D008297:Male; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D056489:Nucleoplasmins; D009865:Oocytes / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D010802:Phylogeny; D011898:Ranidae; D013045:Species Specificity; D013094:Spermatozoa / Q000378:metabolism*; D014981:Xenopus
chemical_list: D002843:Chromatin; D009687:Nuclear Proteins; D056489:Nucleoplasmins; D010750:Phosphoproteins