Expression, purification, and functional characterization of the carboxyl-terminal domain fragment of bacteriophage 434 repressor.
The repressor protein of bacteriophage 434 binds to DNA as a dimer of identical subunits. Its strong dimerization is mediated by the carboxyl-terminal domain. Cooperative interactions between the C-terminal domains of two repressor dimers bound at adjacent sites can stabilize protein-DNA complexes f...
שמור ב:
| הוצא לאור ב: | J Bacteriol |
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| Principais autores: | , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
American Society for Microbiology (ASM)
1994
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC197060/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7961451/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.176.22.6907-6914.1994 |
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