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M9480469.TXT
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1994-08-20
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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).