       Document 0610
 DOCN  M9610610
 TI    Sequence specificity in the higher-order interaction of the Rev protein
       of HIV-1 with its target sequence, the RRE.
 DT    9601
 AU    Powell DM; Zhang MJ; Konings DA; Wingfield PT; Stahl SJ; Dayton ET;
       Dayton AI; Laboratory of Immunoregulation, National Institute of Allergy
       and; Infectious Diseases, National Institute of Health, Bethesda,;
       Maryland 20892, USA.
 SO    J Acquir Immune Defic Syndr Hum Retrovirol. 1995 Nov 1;10(3):317-23.
       Unique Identifier : AIDSLINE MED/96027799
 AB    The Rev protein of human immunodeficiency virus type 1 (HIV-1)
       multimerizes along RNAs containing the Rev target sequence, the RRE.
       Although sequence-specific information is recognized in the high
       affinity or initial interaction, it is not known what role RNA-contained
       information plays in higher-order binding events. We have quantitatively
       studied the binding of Rev protein to the primary Rev binding domain (II
       + III) of wild-type and mutant RREs. RRE mutations that retain the basic
       secondary structure of wild type can separately and differentially alter
       the Kds for formation of the first, second, and third Rev/RRE complexes
       (C1, C2, and C3). The data suggest that Rev recognizes sequence-specific
       information in the RRE when it forms higher-order complexes. However,
       the formation of higher-order complexes is not as dependent on
       sequence-specific information as the first or lowest order binding
       interaction, which involves recognition of the high-affinity site.
 DE    Base Sequence  DNA Probes/CHEMISTRY  Electrophoresis, Agar Gel  Gene
       Products, rev/GENETICS/*METABOLISM  *Genes, env  Human  HIV-1/*GENETICS
       Molecular Sequence Data  Mutation  RNA, Viral/METABOLISM  Support,
       Non-U.S. Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

