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

Citation
Dr. Morcock et al., Role of the histidine residues of visna virus nucleocapsid protein in metal ion and DNA binding, FEBS LETTER, 476(3), 2000, pp. 190-193
Citations number
16
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
476
Issue
3
Year of publication
2000
Pages
190 - 193
Database
ISI
SICI code
0014-5793(20000707)476:3<190:ROTHRO>2.0.ZU;2-Q
Abstract
Zinc finger (ZF) domains in retroviral nucleocapsid proteins usually contai n one histidine per metal ion coordination complex (Cys-X-2-Cys-X-4-His-X-4 -Cys). Visna virus nucleocapsid protein, p8, has two additional histidines (in the second of its two ZFs) that could potentially bind metal ions. Abso rption 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 i n metal ion coordination, and that the two additional histidines appear to interact with nucleic acid bases in p8-DNA complexes. (C) 2000 Federation o f European Biochemical Societies. Published by Elsevier Science B.V. All ri ghts reserved.