Abstract
Proteolytically produced carboxyl-terminal fragments of the human immunodeficiency virus type-1 (HIV-1) Tat protein that include a conserved region rich in arginine and lysine bind specifically to transactivation response RNA sequences (TAR). A chemically synthesized 14-residue peptide spanning the basic subdomain also recognizes TAR, identifying this subdomain as central for RNA interaction. TAR RNA forms a stable hairpin that includes a six-residue loop, a trinucleotide pyrimidine bulge, and extensive duplex structure. Competition and interference experiments show that the Tat-derived fragments bind to double-stranded RNA and interact specifically at the pyrimidine bulge and adjacent duplex of TAR.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding, Competitive
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Gene Products, tat / metabolism*
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HIV-1 / genetics*
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Molecular Sequence Data
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Nucleic Acid Conformation
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Peptide Fragments / isolation & purification
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Peptide Fragments / metabolism
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Peptide Hydrolases
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RNA, Messenger / genetics
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RNA, Messenger / metabolism*
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RNA, Viral / genetics
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RNA, Viral / metabolism*
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Regulatory Sequences, Nucleic Acid / genetics
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Regulatory Sequences, Nucleic Acid / physiology
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Structure-Activity Relationship
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Trans-Activators / metabolism*
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Transcriptional Activation / genetics
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tat Gene Products, Human Immunodeficiency Virus
Substances
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Gene Products, tat
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Peptide Fragments
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RNA, Messenger
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RNA, Viral
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Recombinant Fusion Proteins
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Trans-Activators
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tat Gene Products, Human Immunodeficiency Virus
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Peptide Hydrolases