Bacteriophage T4 regA protein binds RNA as a monomer, overcoming dimer interactions.

The stoichiometry of the complex formed between the T4 translational repressor protein regA and the 16 nt gene 44 recognition element (gene 44RE) RNA has been determined. Under quantitative binding conditions, the association of wild-type regA protein with gene 44RE RNA exhibits saturation at a 1:1...

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Pubblicato in:	Nucleic Acids Res
Autori principali:	Phillips, C A, Gordon, J, Spicer, E K
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	Oxford University Press 1996
Soggetti:	Research Article
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC146235/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8932389/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/24.21.4319
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