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!align=left |Citation | |||
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'''Williams, NL and Maxwell, A''' (1999) Probing the two-gate mechanism of DNA gyrase using cysteine cross-linking. ''Biochemistry'' '''38''':13502-11 | |||
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!align=left |Abstract | |||
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Cross-linking a pair of novel cysteine residues on either side of the bottom dimer interface of DNA gyrase blocks catalytic supercoiling. Limited strand passage is allowed, but release of the transported DNA segment (T segment) via opening of the bottom dimer interface is prevented. In contrast, ATP-independent relaxation of negatively supercoiled DNA is completely abolished, suggesting that T-segment entry via the bottom gate is blocked. These findings support a two-gate model for supercoiling by DNA gyrase and suggest that relaxation by gyrase is the reverse of supercoiling. Cross-linking a truncated version of gyrase (A64(2)B2), which lacks the DNA wrapping domains, does not block ATP-dependent relaxation. This indicates that passage of DNA through the bottom dimer interface is not essential for this reaction. The mechanistic implications of these results are discussed. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10521257 PubMed] | |||
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!align=left |Keywords | |||
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Adenosine Triphosphate/antagonists & inhibitors; Adenosine Triphosphate/chemistry; Calcium/chemistry; Catalysis; Cross-Linking Reagents/chemistry; Cysteine/chemistry; DNA Topoisomerases, Type II/chemistry; DNA Topoisomerases, Type II/genetics; DNA Topoisomerases, Type II/metabolism; DNA, Bacterial/chemistry; DNA, Superhelical/chemistry; Dimerization; Disulfides/chemistry; Escherichia coli/enzymology; Hydrolysis; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Peptide Fragments/chemistry; Peptide Fragments/genetics; Protein Engineering; Quinolones/chemistry | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<annotationlinks/> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
{{LitLinks}} | |||
==See also== | |||
==References== | |||
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<references/> | |||
Latest revision as of 03:52, 8 August 2014
| Citation |
Williams, NL and Maxwell, A (1999) Probing the two-gate mechanism of DNA gyrase using cysteine cross-linking. Biochemistry 38:13502-11 |
|---|---|
| Abstract |
Cross-linking a pair of novel cysteine residues on either side of the bottom dimer interface of DNA gyrase blocks catalytic supercoiling. Limited strand passage is allowed, but release of the transported DNA segment (T segment) via opening of the bottom dimer interface is prevented. In contrast, ATP-independent relaxation of negatively supercoiled DNA is completely abolished, suggesting that T-segment entry via the bottom gate is blocked. These findings support a two-gate model for supercoiling by DNA gyrase and suggest that relaxation by gyrase is the reverse of supercoiling. Cross-linking a truncated version of gyrase (A64(2)B2), which lacks the DNA wrapping domains, does not block ATP-dependent relaxation. This indicates that passage of DNA through the bottom dimer interface is not essential for this reaction. The mechanistic implications of these results are discussed. |
| Links | |
| Keywords |
Adenosine Triphosphate/antagonists & inhibitors; Adenosine Triphosphate/chemistry; Calcium/chemistry; Catalysis; Cross-Linking Reagents/chemistry; Cysteine/chemistry; DNA Topoisomerases, Type II/chemistry; DNA Topoisomerases, Type II/genetics; DNA Topoisomerases, Type II/metabolism; DNA, Bacterial/chemistry; DNA, Superhelical/chemistry; Dimerization; Disulfides/chemistry; Escherichia coli/enzymology; Hydrolysis; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Peptide Fragments/chemistry; Peptide Fragments/genetics; Protein Engineering; Quinolones/chemistry |
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