Document Detail


Phenylacetyl coenzyme A is an effector molecule of the TetR family transcriptional repressor PaaR from Thermus thermophilus HB8.
MedLine Citation:
PMID:  21725002     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Phenylacetic acid (PAA) is a common intermediate in the catabolic pathways of several structurally related aromatic compounds. It is converted into phenylacetyl coenzyme A (PA-CoA), which is degraded to general metabolites by a set of enzymes. Within the genome of the extremely thermophilic bacterium Thermus thermophilus HB8, a cluster of genes, including a TetR family transcriptional regulator, may be involved in PAA degradation. The gene product, which we named T. thermophilus PaaR, negatively regulated the expression of the two operons composing the gene cluster in vitro. T. thermophilus PaaR repressed the target gene expression by binding pseudopalindromic sequences, with a consensus sequence of 5'-CNAACGNNCGTTNG-3', surrounding the promoters. PA-CoA is a ligand of PaaR, with a proposed binding stoichiometry of 1:1 protein monomer, and was effective for transcriptional derepression. Thus, PaaR is a functional homolog of PaaX, a GntR transcriptional repressor found in Escherichia coli and Pseudomonas strains. A three-dimensional structure of T. thermophilus PaaR was predicted by homology modeling. In the putative structure, PaaR adopts the typical three-dimensional structure of the TetR family proteins, with 10 α-helices. A positively charged surface at the center of the molecule is similar to the acyl-CoA-binding site of another TetR family transcriptional regulator, T. thermophilus FadR, which is involved in fatty acid degradation. The CoA moiety of PA-CoA may bind to the center of the PaaR molecule, in a manner similar to the binding of the CoA moiety of acyl-CoA to FadR.
Authors:
Keiko Sakamoto; Yoshihiro Agari; Seiki Kuramitsu; Akeo Shinkai
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-07-01
Journal Detail:
Title:  Journal of bacteriology     Volume:  193     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2011 Sep 
Date Detail:
Created Date:  2011-08-12     Completed Date:  2011-10-06     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4388-95     Citation Subset:  IM    
Affiliation:
RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
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MeSH Terms
Descriptor/Qualifier:
Acetyl Coenzyme A / genetics,  metabolism*
Acyl Coenzyme A / chemistry,  metabolism
Amino Acid Sequence
Bacterial Proteins / genetics,  metabolism*
Biosensing Techniques
Escherichia coli / genetics,  metabolism
Gene Expression Regulation, Bacterial
Genes, Bacterial
Molecular Conformation
Molecular Sequence Data
Multigene Family
Operon
Phenylacetates / metabolism
Recombinant Proteins
Repressor Proteins / genetics,  metabolism*
Reverse Transcriptase Polymerase Chain Reaction
Thermus thermophilus / enzymology,  genetics*
Transcription, Genetic
Chemical
Reg. No./Substance:
0/Acyl Coenzyme A; 0/Bacterial Proteins; 0/Phenylacetates; 0/Recombinant Proteins; 0/Repressor Proteins; 103-82-2/phenylacetic acid; 72-89-9/Acetyl Coenzyme A; 7532-39-0/phenylacetyl-coenzyme A
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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