A mutational analysis of the structural basis for transcriptional activation and monomer-monomer interaction in the TyrR system of Escherichia coli K-12.
In response to the binding of tyrosine or phenylalanine, the TyrR protein (513 amino acids) activates certain promoters and represses others. In a previous study (J. Cui and R. L. Somerville, J. Bacteriol. 175:303-306, 1993), it was shown that promoter activation was selectively abolished in mutant...
محفوظ في:
| الحاوية / القاعدة: | J Bacteriol |
|---|---|
| المؤلفون الرئيسيون: | , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
1993
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC203972/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8449884/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.175.6.1777-1784.1993 |
| الوسوم: |
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