| Transcriptome analysis of agmatine and putrescine catabolism in Pseudomonas aeruginosa PAO1. | |
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MedLine Citation:
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PMID: 18192388 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Polyamines (putrescine, spermidine, and spermine) are major organic polycations essential for a wide spectrum of cellular processes. The cells require mechanisms to maintain homeostasis of intracellular polyamines to prevent otherwise severe adverse effects. We performed a detailed transcriptome profile analysis of Pseudomonas aeruginosa in response to agmatine and putrescine with an emphasis in polyamine catabolism. Agmatine serves as the precursor compound for putrescine (and hence spermidine and spermine), which was proposed to convert into 4-aminobutyrate (GABA) and succinate before entering the tricarboxylic acid cycle in support of cell growth, as the sole source of carbon and nitrogen. Two acetylpolyamine amidohydrolases, AphA and AphB, were found to be involved in the conversion of agmatine into putrescine. Enzymatic products of AphA were confirmed by mass spectrometry analysis. Interestingly, the alanine-pyruvate cycle was shown to be indispensable for polyamine utilization. The newly identified dadRAX locus encoding the regulator alanine transaminase and racemase coupled with SpuC, the major putrescine-pyruvate transaminase, were key components to maintaining alanine homeostasis. Corresponding mutant strains were severely hampered in polyamine utilization. On the other hand, an alternative gamma-glutamylation pathway for the conversion of putrescine into GABA is present in some organisms. Subsequently, GabD, GabT, and PA5313 were identified for GABA utilization. The growth defect of the PA5313 gabT double mutant in GABA suggested the importance of these two transaminases. The succinic-semialdehyde dehydrogenase activity of GabD and its induction by GABA were also demonstrated in vitro. Polyamine utilization in general was proven to be independent of the PhoPQ two-component system, even though a modest induction of this operon was induced by polyamines. Multiple potent catabolic pathways, as depicted in this study, could serve pivotal roles in the control of intracellular polyamine levels. |
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Authors:
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Han Ting Chou; Dong-Hyeon Kwon; Mohamed Hegazy; Chung-Dar Lu |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S. Date: 2008-01-11 |
Journal Detail:
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Title: Journal of bacteriology Volume: 190 ISSN: 1098-5530 ISO Abbreviation: J. Bacteriol. Publication Date: 2008 Mar |
Date Detail:
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Created Date: 2008-02-26 Completed Date: 2008-07-01 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: United States |
Other Details:
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Languages: eng Pagination: 1966-75 Citation Subset: IM |
Affiliation:
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Department of Biology, Georgia State University, 24 Peachtree Center Avenue, Atlanta, GA 30303, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Agmatine
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metabolism* Alanine Racemase / genetics, metabolism Alanine Transaminase / genetics, metabolism Aminohydrolases / genetics, metabolism Bacterial Proteins / genetics, metabolism Gene Expression Profiling / methods* Gene Expression Regulation, Bacterial Genotype Mass Spectrometry Models, Biological Oligonucleotide Array Sequence Analysis Promoter Regions, Genetic / genetics Pseudomonas aeruginosa / genetics*, metabolism* Putrescine / metabolism* Spermidine / metabolism Spermine / metabolism gamma-Aminobutyric Acid / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 110-60-1/Putrescine; 124-20-9/Spermidine; 306-60-5/Agmatine; 56-12-2/gamma-Aminobutyric Acid; 71-44-3/Spermine; EC 2.6.1.2/Alanine Transaminase; EC 3.5.1.-/acetylpolyamine amidohydrolase; EC 3.5.4.-/Aminohydrolases; EC 5.1.1.1/Alanine Racemase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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