FOOTPRINT ANALYSIS OF REPLICATING MURINE LEUKEMIA-VIRUS REVERSE-TRANSCRIPTASE

被引：47

作者：

WOHRL, BM

GEORGIADIS, MM

TELESNITSKY, A

HENDRICKSON, WA

LEGRICE, SFJ

机构：

[1] CASE WESTERN RESERVE UNIV, SCH MED, DIV INFECT DIS, CLEVELAND, OH 44106 USA

[2] RUTGERS STATE UNIV, DEPT CHEM, PISCATAWAY, NJ 08855 USA

[3] RUTGERS STATE UNIV, WAKSMAN INST, PISCATAWAY, NJ 08855 USA

[4] UNIV MICHIGAN, SCH MED, DEPT MICROBIOL & IMMUNOL, ANN ARBOR, MI 48109 USA

[5] COLUMBIA UNIV, HOWARD HUGHES MED INST, DEPT BIOCHEM & MOLEC BIOPHYS, NEW YORK, NY 10032 USA

来源：

SCIENCE | 1995年 / 267卷 / 5194期

关键词：

D O I：

10.1126/science.7528942

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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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页码：96 / 99

页数：4

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