SITE-DIRECTED MUTAGENESIS STUDIES ON THE BINDING OF THE GLOBULAR DOMAIN OF LINKER HISTONE H5 TO THE NUCLEOSOME

被引：20

作者：

BUCKLE, RS ^{[1
]}

MAMAN, JD ^{[1
]}

ALLAN, J ^{[1
]}

机构：

[1] UNIV LONDON KINGS COLL,DEPT BIOPHYS CELL & MOLEC BIOL,DIV BIOMOLEC SCI,26-29 DRURY LANE,LONDON WC2B 5RL,ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 223卷 / 03期

基金：

英国惠康基金;

关键词：

HISTONE-H5; CHROMATIN; NUCLEOSOME; DNA BINDING; SITE-DIRECTED MUTAGENESIS;

D O I：

10.1016/0022-2836(92)90981-O

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：

The globular domain of the linker histone H5 has been expressed in Escherichia coli. The purified peptide is functional as it permits chromatosome protection during micrococcal nuclease digestion of chromatin reconstituted with the peptide, indicating that it binds correctly at the dyad axis of the nucleosomal core particle. The globular domain residue lysine 64 is highly conserved within the linker histone family, and site-directed mutagenesis has been used to assess the importance of this residue in the binding of the globular domain of linker histone H5 to the nucleosome. Recombinant peptides mutated at lysine 64 are unable to elicit chromatosome protection to the same degree as the wild-type peptide, and since they appear to be fully folded, these observations confirm a major role for this residue in determining the effective interaction between the globular domain of histone H5 and the nucleosome. © 1992.

引用

页码：651 / 659

页数：9

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