THE C-DOMAIN IN THE H1 HISTONE IS STRUCTURALLY CONSERVED

被引:19
作者
MAEDER, DL
BOHM, L
机构
[1] UNIV STELLENBOSCH,FAC MED,DEPT RADIOTHERAPY,RADIOBIOL LAB,POB 63,TYGERBERG 7505,SOUTH AFRICA
[2] UNIV CAPE TOWN,DEPT BIOCHEM,CHROMATIN RES CTR,RONDEBOSCH 7700,SOUTH AFRICA
基金
英国医学研究理事会;
关键词
HISTONE H1; C-DOMAIN; COMPOSITION; RESIDUE SPACING; CONSERVATION; HELICITY; SEQUENCE ANALYSIS;
D O I
10.1016/0167-4838(91)90272-2
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 C-domain of H1 is conserved in composition and not in sequence. The following regularities have been identified: the distribution of lysine, alanine and proline is non-random; alanine occurs in doublets and at intervals of 4-6 significantly more often than expected for random sequences of equal composition; and lysine also deviates from random distribution in that doublets are under-represented and intervals of 2-7 are over-represented. Lysine preferentially occurs in singlets and alanine in doublets rather than triplets or quadruplets. This discourages the formation of helices without neutralization of lysine charges. When lysine residues are paired with DNA phosphate residues, helices are highly probable. Interproline spacing promotes short helical segments. The regularities arising from the conservation of composition and non-random residue distribution suggests that C-domains adopt similar structures and in fact are structurally conserved.
引用
收藏
页码:233 / 238
页数:6
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