Fluorescence and nucleic acid binding properties of bovine leukemia virus nucleocapsid protein.
Biophys Chem
; 97(2-3): 203-12, 2002 Jun 19.
Article
em En
| MEDLINE
| ID: mdl-12050010
ABSTRACT
We used the intrinsic fluorescence of bovine leukemia virus p12, a nucleocapsid protein with two tryptophan-containing zinc fingers (ZFs), to study its conformation and binding to single-stranded nucleic acids. Spectral emission maxima suggested solvent-exposed tryptophans. A peptide derived from ZF1 had a higher quantum yield and longer average lifetime (tau) than ZF2. BLV p12 tau and rotational correlation time were greater than ZF values, but all de-metallated sequences gave similar results. Apo p12 showed reduced fluorescence intensity, tau and loss of secondary structure. DNA-binding affinity of p12 was in the nanomolar range, and decreased 14-fold after Zn++ ejection. Nucleobase preference of BLV p12 was different from the closely related HTLV-1 but similar to HIV-1 and SIV nucleocapsids, both phylogenetically distant.
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Base de dados:
MEDLINE
Assunto principal:
DNA de Cadeia Simples
/
Vírus da Leucemia Bovina
/
Proteínas do Nucleocapsídeo
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article