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Updated: Jun 15, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
Published on: January 17, 2025
Rapid propagational interactions of slow binding inhibitor with RecA protein occur on the longer nucleoprotein
1Department of Food and Microbial Technology, Seoul Women's University, Seoul, Republic of Korea. jikim@swu.ac.kr
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[gammaS] may not act simply as a competitive inhibitor, leading to inhibition kinetic patterns that are informative. When a mixture of ATP and ATP[gammaS] 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[gammaS] ratio. This phase consists of a burst or lag in ATP hydrolysis, depending on whether ATP or ATP[gammaS] 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[gammaS] than on shorter DNA cofactors.
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