A COMPLEX PATTERN OF H2A PHOSPHORYLATION IN THE MOUSE TESTIS

被引:13
作者
GREEN, GR
PATEL, JC
HECHT, NB
POCCIA, DL
机构
[1] MT HOLYOKE COLL,DEPT BIOL,S HADLEY,MA 01075
[2] TUFTS UNIV,DEPT BIOL,MEDFORD,MA 02155
关键词
D O I
10.1016/0014-4827(91)90493-E
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
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. © 1991.
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页码:8 / 12
页数:5
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