Isolation and characterization of Rous sarcoma virus recombinant reverse transcriptase dimers.
Reverse transcriptase (RT) preparations containing various molecular forms of the enzyme consisting of alpha- and/or beta-subunits have been isolated from E. coli cells transformed with plasmid pMF14 containing the Rous sarcoma virus (RSV) pol gene. The three possible dimeric forms of the enzyme demonstrated DNA polymerase activity, the relative activities of the alphaalpha, betabeta, and alphabeta forms being about 1:3:4. RNase H activity is associated with the betabeta and alphabeta dimers but not with the alphaalpha dimer. Comparison of the enzymic properties of the various dimers and dissociation--reassociation results suggest that the betabeta and alphabeta dimers of the RSV recombinant reverse transcriptase are similar to the corresponding virion RT forms.
Chernov
A P
AP
Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia. cap@ibpm.serpukhov.su
Koryagin
A V
AV
Ivanov
V A
VA
D001358:Avian Sarcoma Viruses / Q000201:enzymology*; D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D003001:Cloning, Molecular; D019281:Dimerization; D004926:Escherichia coli; D007700:Kinetics; D012194:RNA-Directed DNA Polymerase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013698:Templates, Genetic
D011994:Recombinant Proteins; D012194:RNA-Directed DNA Polymerase