Characterization of nucleosomes consisting of the human testis/sperm-specific histone H2B variant (hTSH2B).
We have reported earlier the occurrence of a specific histone H2B variant in human testis and sperm. Here we have structurally characterized this protein, its association with the rest of the histone octamer, and its effects on the nucleosome structure. We show that a reconstituted octamer consisting of hTSH2B and a stoichiometric complement of histones H2A, H3, and H4 exhibits a lower stability compared to the reconstituted native counterpart consisting of H2B. In contrast, the hTSH2B containing octamers are able to form nucleosome core particles which are structurally and dynamically indistinguishable from those reconstituted with octamers consisting of only native histones. Furthermore, the presence of hTSH2B in the nucleosome does not affect its ability to bind to linker histones.
Li
Andra
A
Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.
Maffey
Allison H
AH
Abbott
Wade D
WD
Conde e Silva
Natalia
N
Prunell
Ariel
A
Siino
Joseph
J
Churikov
Dmitrii
D
Zalensky
Andrei O
AO
Ausió
Juan
J
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D002850:Chromatography, Gel; D014644:Genetic Variation; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D009707:Nucleosomes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012617:Sea Urchins; D013737:Testis / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
D006657:Histones; D009687:Nuclear Proteins; D009707:Nucleosomes; D011994:Recombinant Proteins; C081018:histone H2B type 1-A