DNA transport by a type II topoisomerase: Direct evidence for a two-gate mechanism

Joaquim Roca; James M. Berger; Stephen C. Harrison; James C. Wang

doi:10.1073/pnas.93.9.4057

DNA transport by a type II topoisomerase: Direct evidence for a two-gate mechanism

Joaquim Roca, James M. Berger, Stephen C. Harrison, James C. Wang

Research output: Contribution to journal › Article › peer-review

152 Scopus citations

Abstract

Recent biochemical and crystallographic results suggest that a type II DNA topoisomerase acts as an ATP-modulated clamp with two sets of jaws at opposite ends: a DNA-bound enzyme can admit a second DNA through one set of jaws; upon binding ATP, this DNA is passed through an enzyme-mediated opening in the first DNA and expelled from the enzyme through the other set of jaws. Experiments based on the introduction of reversible disulfide links across one dimer interface of yeast DNA topoisomerase II have confirmed this mechanism. The second DNA is found to enter the enzyme through the gate formed by the N-terminal parts of the enzyme and leave it through the gate close to the C termini.

Original language	English (US)
Pages (from-to)	4057-4062
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	93
Issue number	9
DOIs	https://doi.org/10.1073/pnas.93.9.4057
State	Published - Apr 30 1996
Externally published	Yes

Keywords

DNA topology
disulfide crosslinking
enzyme mechanism
protein engineering

ASJC Scopus subject areas

General

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10.1073/pnas.93.9.4057

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abstract = "Recent biochemical and crystallographic results suggest that a type II DNA topoisomerase acts as an ATP-modulated clamp with two sets of jaws at opposite ends: a DNA-bound enzyme can admit a second DNA through one set of jaws; upon binding ATP, this DNA is passed through an enzyme-mediated opening in the first DNA and expelled from the enzyme through the other set of jaws. Experiments based on the introduction of reversible disulfide links across one dimer interface of yeast DNA topoisomerase II have confirmed this mechanism. The second DNA is found to enter the enzyme through the gate formed by the N-terminal parts of the enzyme and leave it through the gate close to the C termini.",

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T2 - Direct evidence for a two-gate mechanism

AU - Roca, Joaquim

AU - Berger, James M.

AU - Harrison, Stephen C.

AU - Wang, James C.

PY - 1996/4/30

Y1 - 1996/4/30

N2 - Recent biochemical and crystallographic results suggest that a type II DNA topoisomerase acts as an ATP-modulated clamp with two sets of jaws at opposite ends: a DNA-bound enzyme can admit a second DNA through one set of jaws; upon binding ATP, this DNA is passed through an enzyme-mediated opening in the first DNA and expelled from the enzyme through the other set of jaws. Experiments based on the introduction of reversible disulfide links across one dimer interface of yeast DNA topoisomerase II have confirmed this mechanism. The second DNA is found to enter the enzyme through the gate formed by the N-terminal parts of the enzyme and leave it through the gate close to the C termini.

AB - Recent biochemical and crystallographic results suggest that a type II DNA topoisomerase acts as an ATP-modulated clamp with two sets of jaws at opposite ends: a DNA-bound enzyme can admit a second DNA through one set of jaws; upon binding ATP, this DNA is passed through an enzyme-mediated opening in the first DNA and expelled from the enzyme through the other set of jaws. Experiments based on the introduction of reversible disulfide links across one dimer interface of yeast DNA topoisomerase II have confirmed this mechanism. The second DNA is found to enter the enzyme through the gate formed by the N-terminal parts of the enzyme and leave it through the gate close to the C termini.

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KW - enzyme mechanism

KW - protein engineering

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DNA transport by a type II topoisomerase: Direct evidence for a two-gate mechanism

Abstract

Keywords

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