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Science 6 January 1995:
Vol. 267. no. 5194, pp. 96 - 99
DOI: 10.1126/science.7528942
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Articles

Science, Vol 267, Issue 5194, 96-99
Copyright © 1995 by American Association for the Advancement of Science

articles

Footprint analysis of replicating murine leukemia virus reverse transcriptase

BM Wohrl, MM Georgiadis, A Telesnitsky, WA Hendrickson, and SF Le Grice

Division of Infectious Diseases, Case Western Reserve University School of Medicine, Cleveland, OH 44106.

Replication complexes that contained either murine leukemia virus reverse transcriptase (MLV RT) or a variant reverse transcriptase without a ribonuclease (RNase) H domain (delta RH MLV RT) were visualized by enzymatic footprinting. Wild-type MLV RT protected template nucleotides +6 to -27, and primer nucleotides -1 to -26 of primers that had first been extended by one or four nucleotides. Although it catalyzed DNA synthesis, delta RH MLV RT stably bound template-primer only under conditions of reduced ionic strength and protected the duplex portion only as far as position -15. Despite altered hydrolysis profiles, both enzymes covered primarily the template-primer duplex, contradicting recent predictions based on the structure of rat DNA polymerase beta.


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