Literature DB >> 21804007

Most mutant OccR proteins that are defective in positive control hold operator DNA in a locked high-angle bend.

Ching-Sung Tsai1, Chia-Sui Chen, Stephen C Winans.   

Abstract

OccR is a LysR-type transcriptional regulator of Agrobacterium tumefaciens that positively regulates the octopine catabolism operon of the Ti plasmid. Positive control of the occ genes occurs in response to octopine, a nutrient released from crown gall tumors. OccR also functions as an autorepressor in the presence or absence of octopine. OccR binds to a site between occQ and occR in the presence or absence of octopine, although octopine triggers a conformational change that shortens the DNA footprint and relaxes a DNA bend. In order to determine the roles of this conformational change in transcriptional activation, we isolated 11 OccR mutants that were defective in activation of the occQ promoter but were still capable of autorepression. The mutations in these mutants spanned most of the length of the protein. Two additional positive-control mutants were isolated using site-directed mutagenesis. Twelve mutant proteins displayed a high-angle DNA bend in the presence or absence of octopine. One mutant, the L26A mutant, showed ligand-responsive DNA binding similar to that of wild-type OccR and therefore must be impaired in a subsequent step in activation.

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Year:  2011        PMID: 21804007      PMCID: PMC3187433          DOI: 10.1128/JB.05352-11

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  40 in total

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Review 3.  Agrobacterium in the genomics age.

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5.  Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.

Authors:  Nick Quade; Marieke Dieckmann; Matthias Haffke; Ann Kathrin Heroven; Petra Dersch; Dirk W Heinz
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Authors:  R Tyrrell; K H Verschueren; E J Dodson; G N Murshudov; C Addy; A J Wilkinson
Journal:  Structure       Date:  1997-08-15       Impact factor: 5.006

7.  Mutational analysis of the transcriptional regulator GcvA: amino acids important for activation, repression, and DNA binding.

Authors:  A D Jourdan; G V Stauffer
Journal:  J Bacteriol       Date:  1998-09       Impact factor: 3.490

8.  Structural studies on the full-length LysR-type regulator TsaR from Comamonas testosteroni T-2 reveal a novel open conformation of the tetrameric LTTR fold.

Authors:  Dominique Monferrer; Tewes Tralau; Michael A Kertesz; Ina Dix; Maria Solà; Isabel Usón
Journal:  Mol Microbiol       Date:  2010-01-05       Impact factor: 3.501

9.  Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation.

Authors:  Xiaohong Zhou; Zhiyong Lou; Sheng Fu; Anqi Yang; Hongbo Shen; Zexuan Li; Yingji Feng; Mark Bartlam; Honghai Wang; Zihe Rao
Journal:  J Mol Biol       Date:  2009-12-28       Impact factor: 5.469

10.  The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators.

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  2 in total

1.  Crystal structure of the ligand-binding domain of a LysR-type transcriptional regulator: transcriptional activation via a rotary switch.

Authors:  Youngchang Kim; Gekleng Chhor; Ching-Sung Tsai; James B Winans; Robert Jedrzejczak; Andrzej Joachimiak; Stephen C Winans
Journal:  Mol Microbiol       Date:  2018-11       Impact factor: 3.501

2.  The solution configurations of inactive and activated DntR have implications for the sliding dimer mechanism of LysR transcription factors.

Authors:  Michael Lerche; Cyril Dian; Adam Round; Rosa Lönneborg; Peter Brzezinski; Gordon A Leonard
Journal:  Sci Rep       Date:  2016-01-28       Impact factor: 4.379

  2 in total

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