Site-directed alterations in the ATP-binding domain of rho protein affect its activities as a termination factor.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference41 articles.
1. Escherichia coli transcription termination factor rho has a two-domain structure in its activated form.
2. Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination.
3. Transcription termination factor rho is an RNA-DNA helicase
4. Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.
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