| Title |
Rapid Propagational Interactions of Slow Binding Inhibitor with RecA Protein Occur on the Longer Nucleoprotein Filaments |
| Author |
Jong-Il Kim |
| Address |
Department of Food and Microbial Technology, Seoul Women’s University, Seoul 139-774, Republic of Korea |
| Bibliography |
Journal of Microbiology, 48(1),71-76, 2010,
|
| DOI |
|
| Key Words |
adenosine-5′-O-(3-thiotriphosphate), cooperative binding, slow binding inhibitor, DNA-dependent ATPase, RecA protein |
| Abstract |
RecA protein is a DNA-dependent ATPase. RecA protein-mediated ATP hydrolysis occurs throughout the filamentous nucleoprotein complexes of RecA and DNA. Nucleotide analog ATP[γS] may not act simply as a competitive inhibitor, leading to inhibition kinetic patterns that are informative. When a mixture of ATP and ATP[γS] is present at the beginning of reaction, a transient phase lasting several minutes is observed in which the system approaches the state characteristic of the new ATP/ATP[γS] ratio. This phase consists of a burst or lag in ATP hydrolysis, depending on whether ATP or ATP[γS] respectively, is added first. The transition phase reflects a slow conformational change in a RecA monomer or a general adjustment in the structure of RecA filaments. The RecA filaments formed on longer DNA cofactor were more sensitive, and respond more rapidly to ATP[γS] than on shorter DNA cofactors. |
