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J Biol Chem, Vol. 274, Issue 37, 26329-26336, September 10, 1999
From the Max-Planck-Institut für molekulare Physiologie,
Abteilung Physikalische Biochemie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
Reverse transcriptase (RT) isolated from Rous
sarcoma virus (RSV) consists of heterodimeric RT
Soluble Rous Sarcoma Virus Reverse Transcriptases
, 
,
and Purified from Insect Cells Are Processive DNA
Polymerases That Lack an RNase H 3' 
5' Directed Processing
Activity
, RT, and
RT. The subunit (63 kDa) contains an N-terminal polymerase and a
C-terminal RNase H domain. The N terminus of (95 kDa) corresponds
to with the integrase domain attached to the C terminus (32 kDa).
We have constructed baculoviruses expressing the genes for or or the entire pol (99 kDa). Infection of insect cells with
recombinant virus yielded highly active and soluble RSV RT enzymes that
could be purified to >90% homogeneity. HPLC gel filtration showed
that is a dimeric enzyme that can be partially monomerized upon the addition of 45% Me2SO. DNA synthesis on DNA-DNA and
DNA-RNA primer-templates in the presence of competitor substrates
revealed that and as well as are processive polymerases.
However, the affinity of and for primer-template substrates
appears to be higher than that of . All RSV enzymes investigated
have the potential to displace RNA-RNA duplexes more efficiently than
human immunodeficiency virus type 1 RT. Unlike human immunodeficiency
virus type 1 RT, RSV RTs can catalyze an initial RNase H
endonucleolytic cleavage of the RNA template but not a 3' 
5'
directed processing activity.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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