CONTACT SITE OF HISTONE-2A AND HISTONE-2B IN CHROMATIN AND IN SOLUTION

被引：11

作者：

CALLAWAY, JE

DELANGE, RJ

MARTINSON, HG

机构：

[1] UNIV CALIF LOS ANGELES, SCH MED, DEPT BIOL CHEM, LOS ANGELES, CA 90024 USA

[2] UNIV CALIF LOS ANGELES, INST MOLEC BIOL, LOS ANGELES, CA 90024 USA

[3] UNIV CALIF LOS ANGELES, DEPT CHEM & BIOCHEM, LOS ANGELES, CA 90024 USA

来源：

BIOCHEMISTRY | 1985年 / 24卷 / 11期

关键词：

D O I：

10.1021/bi00332a014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Irradiation of isolated nuclei or of a complex of histones 2A (H2A) and 2B (H2B) with UV light produces a covalent cross-link between H2A and H2B. Sequence analysis of the peptides isolated from the H2A-H2B dimer formed in solution and in nuclei demonstrated that both dimers are produced through the covalent linage of Tyr-40 and H2B and Pro-26 of H2A. Tyrosyl residues proximal to Tyr-40 did not produce a cross-link with H2A, thereby indicating that strict conformational parameters are required for production of the H2A-H2B cross-link. The precise juxtaposition of Tyr-40 of H2B and Pro-26 of H2A in this region of the H2A/H2B contact site evidently is not altered upon interaction of these histones with H3 and H4 (tetramer), DNA or other chromosomal components during nucleosome assembly.

引用

页码：2686 / 2692

页数：7

共 36 条

[1] PURIFICATION OF 5 MAIN CALF THYMUS HISTONE FRACTIONS BY GEL EXCLUSION CHROMATOGRAPHY [J].