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Second-site rho mutation: genetic linkage and polyC-dependent ATPase.
Molecular & General Genetics : MGG
|January 1, 1980
Summary
The sur-38 mutation in Escherichia coli suppresses rho-115 defects and affects the rho gene's structure. Rho protein from the double mutant shows extreme heat lability, indicating altered function.
Area of Science:
- Molecular Biology
- Bacterial Genetics
- Protein Biochemistry
Background:
- The Rho transcription termination factor is crucial for bacterial gene regulation.
- Mutations in the rho gene can lead to altered termination efficiency and cellular phenotypes.
Purpose of the Study:
- To characterize the Rho protein purified from different Escherichia coli mutants.
- To investigate the effect of the sur-38 mutation on Rho protein function and stability.
Main Methods:
- Purification of Rho protein from rho-115 sur-38, rho6, and rho-115 mutant strains of E. coli.
- Assay of polyC-dependent ATPase activity.
- Assessment of heat lability of Rho protein preparations.
- Transduction analysis to determine gene linkage.
Main Results:
- Rho protein from rho-115 sur-38 double mutant exhibited extreme heat lability compared to rho-115 and wild-type.
- All purified Rho preparations showed similar polyC-dependent ATPase specific activities.
- Transduction mapping indicated close linkage between sur-38 and rho-115.
Conclusions:
- The sur-38 mutation likely affects the structural gene for Rho, altering its heat stability.
- Suppression of rho-115 phenotype by sur-38 suggests functional interaction or direct effect on Rho structure.