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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
1991-2-7
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pubmed:abstractText |
The structural and functional properties of the nucleocapsid (NC) protein of the avian myeloblastosis virus were examined by steady-state fluorescence and fluorescence anisotropy measurements of the complex between the NC and the extrinsic fluorophore 4,4'-bis(phenylamino)(1,1'-binaphthalene)-5,5'-disulfonic acid (bis-ANS). The intrinsic fluorescence of bis-ANS is enhanced many fold upon forming a complex with the NC. Between 2 and 10 molecules of bis-ANS bind strongly to the NC, with an overall Kd of less than 10(-6) M. The emission of bis-ANS in the complex can also be induced by excitation at 298 nm, indicating that energy is transferred from Trp 80, the sole tryptophan in the NC protein, to bis-ANS. The energy transferred between the Trp 80 and bis-ANS was analyzed to yield a calculated distance of separation between these fluorophores of 28 +/- 3 A; thus, Trp 80 is well removed from the nearest bound bis-ANS. The fluorescence emission of bis-ANS in the NC.bis-ANS complex is efficiently quenched by added salts and by poly(A), suggesting that salt (presumably anions), nucleic acid, and bis-ANS bind to the same, positively charged region on the NC protein. A site size of six nucleotides was determined for nucleic acid binding to the NC protein, with an estimated Kd of less than 10(-6) M. Salt (anion) binding is strong, but nonspecific, with a Kapp of 4 mM, raising the possibility that anion binding to the NC protein might regulate the interaction of the NC with viral RNA inside the host cell.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5,5'-bis(8-(phenylamino)-1-naphthale...,
http://linkedlifedata.com/resource/pubmed/chemical/Anilino Naphthalenesulfonates,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/Retroviridae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Core Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/avian retrovirus proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7991-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2261456-Amino Acid Sequence,
pubmed-meshheading:2261456-Anilino Naphthalenesulfonates,
pubmed-meshheading:2261456-Binding Sites,
pubmed-meshheading:2261456-Capsid,
pubmed-meshheading:2261456-Fluorescence Polarization,
pubmed-meshheading:2261456-Fluorescent Dyes,
pubmed-meshheading:2261456-Molecular Sequence Data,
pubmed-meshheading:2261456-Nucleic Acids,
pubmed-meshheading:2261456-Poly A,
pubmed-meshheading:2261456-Retroviridae Proteins,
pubmed-meshheading:2261456-Sodium Chloride,
pubmed-meshheading:2261456-Spectrometry, Fluorescence,
pubmed-meshheading:2261456-Structure-Activity Relationship,
pubmed-meshheading:2261456-Viral Core Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
Interactions at the nucleic acid binding site of the avian retroviral nucleocapsid protein: studies utilizing the fluorescent probe 4,4'-bis(phenylamino)(1,1'-binaphthalene)-5,5'-disulfonic acid.
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pubmed:affiliation |
Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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