Role of the histidine residues of visna virus nucleocapsid protein in metal ion and DNA binding

FEBS Letters

Casas-Finet, José R.¹  Morcock, David R.¹  Sowder, Raymond C.¹ 

[1] AIDS Vaccine Program, SAIC Frederick, National Cancer Institute–Frederick Cancer Research and Development Center, Building 535-4, P.O. Box B, Frederick, MD 21702, USA

关键词: Histidine residues;    Visna virus nucleocapsid protein;    Metal ion binding;    DNA binding;    Zinc finger domains;   

DOI  :  10.1016/S0014-5793(00)01723-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Zinc finger (ZF) domains in retroviral nucleocapsid proteins usually contain one histidine per metal ion coordination complex (Cys-X₂-Cys-X₄-His-X₄-Cys). Visna virus nucleocapsid protein, p8, has two additional histidines (in the second of its two ZFs) that could potentially bind metal ions. Absorption spectra of cobalt-bound ZF2 peptides were altered by Cys alkylation and mutation, but not by mutation of the extra histidines. Our results show that visna p8 ZFs involve three Cys and one His in the canonical spacing in metal ion coordination, and that the two additional histidines appear to interact with nucleic acid bases in p8–DNA complexes.

【 授权许可】

Unknown