title: A complex pattern of H2A phosphorylation in the mouse testis.
abstract: Phosphorylation of H2A histones in mouse testis was examined using testis tubule cultures labeled with 32PO4. Histones were analyzed by two systems of two-dimensional polyacrylamide gel electrophoresis, followed by autoradiography of the gels. Of the 32PO4 detected in histones, 95% was incorporated by certain modified forms of the H2A variants H2A.1 and H2A.X. Phosphorylation sites were mapped to N- and C-terminal regions of the modified variants by SDS gel electrophoresis and autoradiography of peptides generated by cleavage of in vitro-labeled proteins with N-bromosuccinimide. Incorporation rates differed for N- and C-terminal regions from different modified forms, demonstrating a complex pattern of H2A phosphorylation in the mouse testis.
authors.affiliation: Biology Department, Amherst College, Massachusetts 01002.
authors.forename: G R
authors.initials: GR
authors.lastname: Green
authors.forename: J C
authors.initials: JC
authors.lastname: Patel
authors.forename: N B
authors.initials: NB
authors.lastname: Hecht
authors.forename: D L
authors.initials: DL
authors.lastname: Poccia
mesh_terms: D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008297:Male; D051379:Mice; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D013737:Testis / Q000378:metabolism*
chemical_list: D006657:Histones; D010750:Phosphoproteins; D010768:Phosphoserine