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Role of the histidine residues of visna virus nucleocapsid protein in metal ion and DNA binding
Author(s) -
Morcock David R.,
Sowder Raymond C.,
Casas-Finet José R.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01723-3
Subject(s) - histidine , chemistry , dna , nucleic acid , metal , zinc finger , metal ions in aqueous solution , zinc , amino acid , crystallography , stereochemistry , biochemistry , organic chemistry , transcription factor , gene
Zinc finger (ZF) domains in retroviral nucleocapsid proteins usually contain 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. 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.