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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
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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

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