Linked Life Data

21081095

Source:http://linkedlifedata.com/resource/pubmed/id/21081095

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-11-18
pubmed:abstractText
We report a comparative study in which a single-molecule fluorescence resonance energy transfer approach was used to examine how the binding of two families of HIV-1 viral proteins to viral RNA hairpins locally changes the RNA secondary structures. The single-molecule fluorescence resonance energy transfer results indicate that the zinc finger protein (nucleocapsid) locally melts the TAR RNA and RRE-IIB RNA hairpins, whereas arginine-rich motif proteins (Tat and Rev) may strengthen the hairpin structures through specific binding interactions. Competition experiments show that Tat and Rev can effectively inhibit the nucleocapsid-chaperoned annealing of complementary DNA oligonucleotides to the TAR and RRE-IIB RNA hairpins, respectively. The competition binding data presented here suggest that the specific nucleic acid binding interactions of Tat and Rev can effectively compete with the general nucleic acid binding/chaperone functions of the nucleocapsid protein, and thus may in principle help regulate critical events during the HIV life cycle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1542-0086
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
17
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3454-62
pubmed:meshHeading
pubmed-meshheading:21081095-Amino Acid Sequence, pubmed-meshheading:21081095-Arginine, pubmed-meshheading:21081095-Base Sequence, pubmed-meshheading:21081095-Electrophoretic Mobility Shift Assay, pubmed-meshheading:21081095-Fluorescence Resonance Energy Transfer, pubmed-meshheading:21081095-HIV Long Terminal Repeat, pubmed-meshheading:21081095-HIV-1, pubmed-meshheading:21081095-Kinetics, pubmed-meshheading:21081095-Molecular Sequence Data, pubmed-meshheading:21081095-Nucleic Acid Conformation, pubmed-meshheading:21081095-Nucleocapsid Proteins, pubmed-meshheading:21081095-Protein Binding, pubmed-meshheading:21081095-RNA, Viral, pubmed-meshheading:21081095-Response Elements, pubmed-meshheading:21081095-Zinc Fingers, pubmed-meshheading:21081095-rev Gene Products, Human Immunodeficiency Virus, pubmed-meshheading:21081095-tat Gene Products, Human Immunodeficiency Virus
pubmed:year
2010
pubmed:articleTitle
Comparative analysis of RNA/protein dynamics for the arginine-rich-binding motif and zinc-finger-binding motif proteins encoded by HIV-1.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of Texas, Austin, TX, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural