A NOVEL ARRANGEMENT OF ZINC-BINDING RESIDUES AND SECONDARY STRUCTURE IN THE C3HC4 MOTIF ON AN ALPHA HERPES-VIRUS PROTEIN FAMILY

被引:110
作者
EVERETT, RD
BARLOW, P
MILNER, A
LUISI, B
ORR, A
HOPE, G
LYON, D
机构
[1] UNIV OXFORD, DEPT BIOCHEM, OXFORD, ENGLAND
[2] GLASGOW ROYAL INFIRM, DEPT BIOCHEM, GLASGOW G4 0SF, SCOTLAND
关键词
C3HC4; MOTIF; ZINC FINGER; HERPES VIRUS; VMW110;
D O I
10.1006/jmbi.1993.1657
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
A highly conserved, cysteine-rich region plays a crucial role in the function of a family of regulatory proteins encoded by alpha herpes viruses. The so-called C3HC4 motif spans approximately 60 residues and has been predicted to bind zinc. This motif occurs in a number of other viral and cellular proteins, many of which appear to be involved in some aspect of the regulation of gene expression. We have cloned and expressed in bacteria a portion of immediate-early protein Vmw110 of herpes simplex virus type 1 that encompasses the C3HC4 motif, and the equivalent regions from the homologous proteins of varicella zoster virus and equine herpes virus type 1 (EHV-1). All three polypeptides were purified and found to bind zinc stably. None of the three interacted significantly with either DNA or RNA under our assay conditions. The EHV-1 domain yielded interpretable proton nuclear magnetic resonance spectra. Assignment of resonances and analysis of nuclear Overhauser effects revealed its secondary structure. Starting from the N terminus, this consists of an ordered but irregular loop, the first two strands of a triple-stranded antiparallel β-sheet, two turns of an α-helix, a second irregular loop, and the third strand of the β-sheet. It appears that, taking the cysteine and histidine residues in turn, cysteine residues I, II, IV and V co-ordinate one zinc atom while the histidine residue and cysteine residues III, VI and VII co-ordinate a second zinc atom. This arrangement of secondary structure differs from that found in other characterized zinc-containing proteins. © 1993 Academic Press Limited.
引用
收藏
页码:1038 / 1047
页数:10
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