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

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 i...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1996-04, Vol.93 (9), p.4057-4062
Hauptverfasser:	Roca, J. (Harvard University, Cambridge, MA.), Berger, J.M, Harrison, S.C, Wang, J.C
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ADENOSINE TRIPHOSPHATE Adenosine Triphosphate - metabolism ADENOSINTRIFOSFATO Adenylyl Imidodiphosphate - pharmacology ADN Binding Sites Biochemistry Computer Graphics Computer Simulation Cross-Linking Reagents Deoxyribonucleic acid Dimers Disulfides DNA DNA Topoisomerases, Type II - chemistry DNA Topoisomerases, Type II - metabolism DNA, Single-Stranded - chemistry DNA, Single-Stranded - metabolism Electrophoresis Enzymes Gels ISOMERASAS ISOMERASE Macromolecular Substances Mathematical rings Models, Molecular Nucleic Acid Conformation Plasmids Point Mutation Protein Structure, Secondary Proteins REACCIONES QUIMICAS REACTION CHIMIQUE Recombinant Proteins - chemistry Recombinant Proteins - metabolism SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology TRANSPORT TRANSPORTE Yeasts
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Beschreibung
Zusammenfassung:	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.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.93.9.4057