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A single aromatic residue in transcriptional repressor protein KorA is critical for cooperativity with its co-regulator KorB

Bingle, Lewis E. H. and Rajasekar, Karthik V. and Muntaha, Sidra tul and Nadella, Vinod and Hyde, Eva I. and Thomas, Christopher M. (2008) A single aromatic residue in transcriptional repressor protein KorA is critical for cooperativity with its co-regulator KorB. Molecular Microbiology, 70 (6). pp. 1502-1514. ISSN 1502–1514

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URL of Published Version: http://www3.interscience.wiley.com/cgi-bin/fulltext/121462431/PDFSTART

Identification Number/DOI: 10.1111/j.1365-2958.2008.06498.x

A central feature of broad host range IncP-1 plasmids is the set of regulatory circuits that tightly control plasmid core functions under steady-state conditions. Cooperativity between KorB and either KorA or TrbA repressor proteins is a key element of these circuits and deletion analysis has implicated the conserved C-terminal domain of KorAand TrbAin this interaction. By NMR we show that KorA and KorB interact directly and identify KorA amino acids that are affected on KorB binding. Studies on mutants showed that tyrosine 84 (or phenylalanine, in some alleles) is dispensable for repressor activity but critical for the specific interaction with KorB in both in vivo reporter gene assays and in vitro electrophoretic mobility shift and co-purification assays. This confirms that direct and specific protein–protein interactions are responsible for the cooperativity observed between KorB and its corepressors and lays the basis for determining the
biological importance of this cooperativity.

Type of Work:Article
Date:20 October 2008 (Publication)
School/Faculty:Colleges (2008 onwards) > College of Life & Environmental Sciences
Department:School of Biosciences
Subjects:QR Microbiology
Institution:University of Birmingham
Copyright Holders:Blackwell Publishing
ID Code:115
Refereed:YES
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