Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-13T04:10:52.559Z Has data issue: false hasContentIssue false
  • English
  • Français

Temperature-sensitive suppressor mutations of the Escherichia coli DNA gyrase B protein

Published online by Cambridge University Press:  01 May 2000

STEPHEN J. BLANCE ,
NICOLA L. WILLIAMS ,
ZOË A. PRESTON ,
JOHN BISHARA ,
MICHAEL S. SMYTH  and
ANTHONY MAXWELL
STEPHEN J. BLANCE
Affiliation:
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom
NICOLA L. WILLIAMS
Affiliation:
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom
ZOË A. PRESTON
Affiliation:
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom
JOHN BISHARA
Affiliation:
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom
MICHAEL S. SMYTH
Affiliation:
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom
ANTHONY MAXWELL
Affiliation:
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom
Get access

Abstract

Escherichia coli strain LE316 contains a mutation in gyrB that results in the substitution of Val164 to Gly and confers both chlorobiocin resistance and temperature sensitivity. Selection for suppressors of the ts phenotype yielded second-site mutations in GyrB at His38 and Thr157. The properties of proteins bearing these mutations have been characterized, and a mechanism of suppression is proposed based upon structural considerations.

Keywords

coumaringyrasenovobiocinsuppressortopoisomerase
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 5 , May 2000 , pp. 1035 - 1037
Copyright
2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)