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Western University

Bacterial Proteins

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Oligomerization Of Benm, A Lysr-Type Transcriptional Regulator: Structural Basis For The Aggregation Of Proteins In This Family., Obidimma Ezezika, Sandra Haddad, Ellen L Neidle, Cory Momany May 2007

Oligomerization Of Benm, A Lysr-Type Transcriptional Regulator: Structural Basis For The Aggregation Of Proteins In This Family., Obidimma Ezezika, Sandra Haddad, Ellen L Neidle, Cory Momany

Health Studies Publications

LysR-type transcriptional regulators comprise the largest family of homologous regulatory DNA-binding proteins in bacteria. A problematic challenge in the crystallization of LysR-type regulators stems from the insolubility and precipitation difficulties encountered with high concentrations of the full-length versions of these proteins. A general oligomerization scheme is proposed for this protein family based on the structures of the effector-binding domain of BenM in two different space groups, P4(3)22 and C222(1). These structures used the same oligomerization scheme of dimer-dimer interactions as another LysR-type regulator, CbnR, the full-length structure of which is available [Muraoka et al. (2003), J. Mol. Biol. 328, 555-566]. …


Catm Regulation Of The Benabcde Operon: Functional Divergence Of Two Lysr-Type Paralogs In Acinetobacter Baylyi Adp1., Obidimma Ezezika, Lauren S Collier-Hyams, Haley A Dale, Andrew C Burk, Ellen L Neidle Mar 2006

Catm Regulation Of The Benabcde Operon: Functional Divergence Of Two Lysr-Type Paralogs In Acinetobacter Baylyi Adp1., Obidimma Ezezika, Lauren S Collier-Hyams, Haley A Dale, Andrew C Burk, Ellen L Neidle

Health Studies Publications

Two LysR-type transcriptional regulators, BenM and CatM, control benzoate consumption by the soil bacterium Acinetobacter baylyi ADP1. These homologs play overlapping roles in the expression of multiple genes. This study focuses on the benABCDE operon, which initiates benzoate catabolism. At this locus, BenM and CatM each activate transcription in response to the catabolite cis,cis-muconate. BenM, but not CatM, additionally responds to benzoate as an effector. Regulation by CatM alone is insufficient for growth on benzoate as the sole carbon source. However, three point mutations independently increased CatM-activated benA transcription and enabled growth on benzoate without BenM. Two mutations generate variants …