Document 0200
 DOCN  M9580200
 TI    An expanded model of replicating human immunodeficiency virus reverse
       transcriptase.
 DT    9506
 AU    Wohrl BM; Tantillo C; Arnold E; Le Grice SF; Division of Infectious
       Diseases, Case Western Reserve University; School of Medicine,
       Cleveland, Ohio 44106, USA.
 SO    Biochemistry. 1995 Apr 25;34(16):5343-56. Unique Identifier : AIDSLINE
       MED/95244457
 AB    Replication complexes containing wild-type and RNase H-deficient p66/p51
       human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT)
       were analyzed by DNase I and S1 footprinting. While crystallography and
       chemical footprinting data demonstrate that 15-18 bases of primer and
       template occupy the DNA polymerase and RNase H active centers, enzymatic
       footprinting suggests that a larger portion of substrate is encompassed
       by the replicating enzyme. Independent of the position of DNA synthesis
       arrest, template nucleotides +7 to -23 and primer nucleotides -1 to -25
       are nuclease resistant. On both DNA strands, position -20 remains
       accessible to DNase I cleavage, suggestive of an alteration in nucleic
       acid structure between exiting the RNase H catalytic center and leaving
       the C-terminal p66 domain. A model of HIV-1 RT containing an extended
       single-stranded template and duplex region was constructed on the basis
       of the structure of an RT/DNA complex. Mapping of footprint data onto
       this model shows consistency between biochemical and structural data,
       implicating a contribution from domains proximal to the catalytic
       centers.
 DE    Base Sequence  Binding Sites  Deoxyribonuclease I  DNA
       Polymerases/METABOLISM  DNA Primers  *DNA Replication  DNA,
       Viral/BIOSYNTHESIS/*CHEMISTRY  HIV-1/*ENZYMOLOGY  Models, Molecular
       Molecular Sequence Data  Nucleic Acid Conformation  *Protein
       Conformation  Protein Structure, Secondary  Recombinant
       Proteins/BIOSYNTHESIS/CHEMISTRY/METABOLISM  Reverse
       Transcriptase/BIOSYNTHESIS/*CHEMISTRY/*METABOLISM  Ribonuclease H, Calf
       Thymus/METABOLISM  Substrate Specificity  Support, Non-U.S. Gov't
       Support, U.S. Gov't, P.H.S.  Templates  JOURNAL ARTICLE

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