Document 0450
 DOCN  M9590450
 TI    Structural variety of arginine-rich RNA-binding peptides.
 DT    9509
 AU    Tan R; Frankel AD; Department of Biochemistry and Biophysics, University
       of; California, San Francisco 94141, USA.
 SO    Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5282-6. Unique Identifier :
       AIDSLINE MED/95296294
 AB    Arginine-rich domains are used by a variety of RNA-binding proteins to
       recognize specific RNA hairpins. It has been shown previously that a
       17-aa arginine-rich peptide from the human immunodeficiency virus Rev
       protein binds specifically to its RNA site when the peptide is in an
       alpha-helical conformation. Here we show that related peptides from
       splicing factors, viral coat proteins, and bacteriophage antiterminators
       (the N proteins) also have propensities to form alpha-helices and that
       the N peptides require helical conformations to bind to their cognate
       RNAs. In contrast, introducing proline mutations into the arginine-rich
       domain of the human immunodeficiency virus Tat protein abolishes its
       potential to form an alpha-helix but does not affect RNA-binding
       affinity in vitro or in vivo. Based on results from several peptide-RNA
       model systems, we suggest that helical peptides may be used to recognize
       RNA structures having particularly wide major grooves, such as those
       found near loops or large bulges, and that nonhelical or extended
       peptides may be used to recognize less accessible grooves.
 DE    Amino Acid Sequence  Arginine/*CHEMISTRY/METABOLISM  Circular Dichroism
       Gene Products, tat/CHEMISTRY/METABOLISM  HIV/METABOLISM  Molecular
       Sequence Data  Mutation  Peptides/*CHEMISTRY
       Proline/CHEMISTRY/METABOLISM  Protein Conformation  RNA-Binding
       Proteins/*CHEMISTRY  RNA, Viral/METABOLISM  Support, Non-U.S. Gov't
       Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

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