SITES OF REACTION OF ESCHERICHIA-COLI DNA GYRASE ON PBR322 INVIVO AS REVEALED BY OXOLINIC ACID-INDUCED PLASMID LINEARIZATION
SITES OF REACTION OF ESCHERICHIA-COLI DNA GYRASE ON PBR322 INVIVO AS REVEALED BY OXOLINIC ACID-INDUCED PLASMID LINEARIZATION
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DOI:
10.1016/0022-2836(85)90324-9
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发表时间:
1985-01-01
影响因子:
5.6
通讯作者:
MORRIS, DR
中科院分区:
文献类型:
--
作者:
LOCKSHON, D;MORRIS, DR
pBR322 DNA, linearized by lysis of an oxolinic acid-treated culture of E. coli strain DK6recA- (pBR322) with sodium dodecyl sulfate, was purified, treated with DNA polymerase in the presence of the 4 deoxynucleoside triphosphates, and ligated to DNA linkers containing the XhoI recognition sequence. Most of the drug-resistant colonies resulting from transformation of E. coli with this material bore plasmids that appeared by restriction enzyme analysis to differ from pBR322 only by the introduction of an XhoI site. The XhoI sites in plasmids from 93 transformants were distributed unevenly around the pBR322 map. Maxam-Gilbert DNA sequence analysis of 36 of these plasmids, labeled at the 5'' termini of the XhoI sites, revealed that 29 of them contained, in addition to the XhoI linker, a duplication of 4 base-pairs of the pBR322 sequence surrrounding the linker. Therefore, oxolinic acid-induced linearization must have resulted in 5''-terminal extensions of 4 bases, the configuration known to result from oxolinic acid-induced DNA cleavage by DNA gyrase in vitro. The sequence data thus allowed the determination of the precise point at which linearization occurred, apparently by the abortion of a gyrase-DNA covalent intermediate that existed in vivo. When the 19 different sites of the 29 plasmids were compared, the following set of rules could be derived: .**GRAPHIC**. where N is any nucleotide, R is a purine and Y is a pyrimidine. Cleavage occurred at the line between the 8th and 9th positions from the left. The parenthetical G and T were preferred secondarily to T and G, respectively; T and G in the 13th position from the left were equally preferred. Several of these rules are similar to those proposed previously based on several in vitro gyrase cleavage sites. Some of the rules show dyad symmetry around the axis midway between the cleavage points in the 2 strands, while others are distinctly asymmetric.