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...

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Bibliografiska uppgifter
Huvudupphovsmän: Carlson, P A, Koudelka, G B
Materialtyp: Artigo
Språk:Inglês
Publicerad: 1994
Ämnen:
Research Article
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC197060/
https://ncbi.nlm.nih.gov/pubmed/7961451
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