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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Detaylı Bibliyografya

Yayımlandı:	J Bacteriol
Asıl Yazarlar:	Carlson, P A, Koudelka, G B
Materyal Türü:	Artigo
Dil:	Inglês
Baskı/Yayın Bilgisi:	American Society for Microbiology (ASM) 1994
Konular:	Research Article
Online Erişim:	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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