Document Detail


Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa.
MedLine Citation:
PMID:  16352820     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To circumvent the permeability barrier of its outer membrane, Pseudomonas aeruginosa has evolved a series of specific porins. These channels have binding sites for related classes of molecules that facilitate uptake under nutrient-limited conditions. Here, we report on the identification of a 19-member family of porins similar to the basic-amino-acid-specific porin OprD. The members of this family fell into one of two phylogenetically distinct clusters, one bearing high similarity to OprD and the other bearing most similarity to the putative phenylacetic acid uptake porin PhaK of Pseudomonas putida. Analysis of the genome context, operon arrangement, and regulation of the PhaK-like porin OpdK indicated that it might be involved in vanillate uptake. This result was confirmed by demonstrating that an opdK mutant had a deficiency in the ability to grow on vanillate as a carbon source. To extrapolate these data to other paralogues within this family, the substrate specificities of 6 of the 17 remaining OprD homologues were inferred using an approach similar to that used with opdK. The specificities determined were as follows: OpdP, glycine-glutamate; OpdC, histidine; OpdB, proline; OpdT, tyrosine; OpdH, cis-aconitate; and OpdO, pyroglutamate. Thus, members of the OprD subfamily took up amino acids and related molecules, and those characterized members most similar to PhaK were responsible for the uptake of a diverse array of organic acids. These results imply that there is a functional basis for the phylogenetic clustering of these proteins and provide a framework for studying OprD homologues in other organisms.
Authors:
Sandeep Tamber; Martina M Ochs; Robert E W Hancock
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  188     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2005-12-14     Completed Date:  2006-03-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  45-54     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Immunology, University of British Columbia, No. 235 2259 Lower Mall, Lower Mall Research Station, Vancouver, British Columbia V6T 1Z4, Canada.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism*
Arginine / metabolism
Gene Expression Regulation, Bacterial
Multigene Family*
Phylogeny
Porins / genetics,  metabolism*
Pseudomonas aeruginosa / genetics,  growth & development,  metabolism*
Substrate Specificity
Transcription, Genetic
Vanillic Acid / metabolism
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Porins; 121-34-6/Vanillic Acid; 148412-32-2/OprD protein, Pseudomonas aeruginosa; 74-79-3/Arginine
Comments/Corrections

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


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