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• W1966607206 abstract "ABSTRACT The global regulators AbrB, Abh, and SpoVT are paralogous proteins showing their most extensive sequence homologies in the DNA-binding amino-terminal regions (about 50 residues). The carboxyl-terminal portion of AbrB has been hypothesized to be a multimerization domain with little if any role in DNA-binding recognition or specificity. To investigate the multimerization potentials of the carboxyl-terminal portions of AbrB, Abh, and SpoVT we utilized an in vivo multimerization assay system based upon fusion of the domains to the DNA binding domain of the λ cI repressor protein. The results indicate that the N and C domains of all three paralogues are independent dimerization modules and that the intact Abh and SpoVT proteins are most probably tetramers. Chimeric proteins consisting of the AbrB N-terminal DNA-binding domain fused to the C domain of either Abh or SpoVT are indistinguishable from wild-type AbrB in their ability to regulate an AbrB target promoter in vivo." @default.
• W1966607206 created "2016-06-24" @default.
• W1966607206 creator A5048190784 @default.
• W1966607206 creator A5078423942 @default.
• W1966607206 date "2005-09-15" @default.
• W1966607206 modified "2023-09-27" @default.
• W1966607206 title "Independent and Interchangeable Multimerization Domains of the AbrB, Abh, and SpoVT Global Regulatory Proteins" @default.
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• W1966607206 doi "https://doi.org/10.1128/jb.187.18.6354-6362.2005" @default.
• W1966607206 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1273005" @default.
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