Document 0469
 DOCN  M9480469
 TI    Footprinting RNA-protein complexes following gel retardation assays:
       application to the R-17-procoat-RNA and tat--TAR interactions.
 DT    9410
 AU    Pearson L; Chen CB; Gaynor RP; Sigman DS; Department of Biological
       Chemistry, School of Medicine,; University of California, Los Angeles
       90024-1570.
 SO    Nucleic Acids Res. 1994 Jun 25;22(12):2255-63. Unique Identifier :
       AIDSLINE MED/94310052
 AB    RNA-protein complexes isolated following a gel retardation assay can be
       footprinted within the gel matrix using the chemical nuclease activities
       of 4,7-dimethyl-, 5,6-dimethyl-, and
       3,4,7,8-tetramethyl-1,10-phenanthroline-copper. These complexes are more
       reactive than 1,10-phenanthroline-copper but share its reaction
       preference for bulges and loops. The interaction of the coat protein of
       R-17 with its viral RNA target and tat- and tat-derived peptides with
       HIV TAR RNA have been studied. In both cases, the RNA sequence opposite
       a 2-3 nucleotide bulge are protected. Tat-derived peptides inhibit
       cleavage at sites which intact tat does not protect. These results are
       consistent with transcription studies which have suggested that
       truncation of tat increases nonspecific binding.
 DE    Amino Acid Sequence  Bacterial Proteins/*METABOLISM  Base Sequence
       Capsid/*METABOLISM  Cell Line  Copper/METABOLISM  DNA  Gene Products,
       tat/*METABOLISM  Genetic Techniques  Membrane Proteins/*METABOLISM
       Molecular Sequence Data  Phenanthrolines  Ribonucleases/METABOLISM
       RNA-Binding Proteins/*METABOLISM  RNA, Viral/*METABOLISM  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).