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Genetics of the glutamate‐mediated methylamine utilization pathway in the facultative methylotrophic beta‐proteobacterium Methyloversatilis universalis FAM5

The ability of some microbial species to oxidize monomethylamine via glutamate‐mediated pathways was proposed in the 1960s; however, genetic determinants of the pathways have never been described. In the present study we describe a gene cluster essential for operation of the ‐methylglutamate pathway... Full description

Journal Title: Molecular Microbiology January 2010, Vol.75(2), pp.426-439
Main Author: Latypova, Ekaterina
Other Authors: Yang, Song , Wang, Yi‐Shun , Wang, Tiansong , Chavkin, Theodore A. , Hackett, Murray , Schäfer, Hendrik , Kalyuzhnaya, Marina G.
Format: Electronic Article Electronic Article
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ID: ISSN: 0950-382X ; E-ISSN: 1365-2958 ; DOI: 10.1111/j.1365-2958.2009.06989.x
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recordid: wj10.1111/j.1365-2958.2009.06989.x
title: Genetics of the glutamate‐mediated methylamine utilization pathway in the facultative methylotrophic beta‐proteobacterium Methyloversatilis universalis FAM5
format: Article
creator:
  • Latypova, Ekaterina
  • Yang, Song
  • Wang, Yi‐Shun
  • Wang, Tiansong
  • Chavkin, Theodore A.
  • Hackett, Murray
  • Schäfer, Hendrik
  • Kalyuzhnaya, Marina G.
subjects:
  • Genetic Research -- Analysis
  • Genetic Research -- Genetic Aspects
  • Biopolymers -- Analysis
  • Biopolymers -- Genetic Aspects
  • Enzymology -- Analysis
  • Enzymology -- Genetic Aspects
  • Glutamine -- Analysis
  • Glutamine -- Genetic Aspects
  • Glutamate -- Analysis
  • Glutamate -- Genetic Aspects
  • Oxidases -- Analysis
  • Oxidases -- Genetic Aspects
  • Polypeptides -- Analysis
  • Polypeptides -- Genetic Aspects
  • Ligases -- Analysis
  • Ligases -- Genetic Aspects
ispartof: Molecular Microbiology, January 2010, Vol.75(2), pp.426-439
description: The ability of some microbial species to oxidize monomethylamine via glutamate‐mediated pathways was proposed in the 1960s; however, genetic determinants of the pathways have never been described. In the present study we describe a gene cluster essential for operation of the ‐methylglutamate pathway in the methylotrophic beta‐proteobacterium FAM5. Four major polypeptides from protein fractions displaying high activities of ‐methylglutamate synthetase, ‐methylglutamate dehydrogenase and γ‐glutamylmethylamide synthetase were selected for mass spectrometry‐based identification. The activities of enzymes were associated with the presence of peptides identified as ferredoxin‐dependent glutamate synthase (GltB2), large subunit of putative heterotetrameric sarcosine oxidase (SoxA) and glutamine synthetase type III (GSIII) respectively. A gene cluster (8.3 kb) harbouring and ‐like genes was amplified from FAM5, sequenced and assembled. Two partial and six complete open reading frames arranged in the order were identified and subjected to mutational analysis, functional and metabolic profiling. We demonstrated that ‐like and ‐like genes play a key role in methylamine utilization and encode ‐methylglutamate synthetase and ‐methylglutamate dehydrogenase respectively. Metabolic, enzymatic and mutational analyses showed that the ‐like gene encodes γ‐glutamylmethylamide synthetase; however, this enzyme is not essential for oxidation of methylamine.
language:
source:
identifier: ISSN: 0950-382X ; E-ISSN: 1365-2958 ; DOI: 10.1111/j.1365-2958.2009.06989.x
fulltext: fulltext
issn:
  • 0950-382X
  • 0950382X
  • 1365-2958
  • 13652958
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titleGenetics of the glutamate‐mediated methylamine utilization pathway in the facultative methylotrophic beta‐proteobacterium Methyloversatilis universalis FAM5
creatorLatypova, Ekaterina ; Yang, Song ; Wang, Yi‐Shun ; Wang, Tiansong ; Chavkin, Theodore A. ; Hackett, Murray ; Schäfer, Hendrik ; Kalyuzhnaya, Marina G.
ispartofMolecular Microbiology, January 2010, Vol.75(2), pp.426-439
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descriptionThe ability of some microbial species to oxidize monomethylamine via glutamate‐mediated pathways was proposed in the 1960s; however, genetic determinants of the pathways have never been described. In the present study we describe a gene cluster essential for operation of the ‐methylglutamate pathway in the methylotrophic beta‐proteobacterium FAM5. Four major polypeptides from protein fractions displaying high activities of ‐methylglutamate synthetase, ‐methylglutamate dehydrogenase and γ‐glutamylmethylamide synthetase were selected for mass spectrometry‐based identification. The activities of enzymes were associated with the presence of peptides identified as ferredoxin‐dependent glutamate synthase (GltB2), large subunit of putative heterotetrameric sarcosine oxidase (SoxA) and glutamine synthetase type III (GSIII) respectively. A gene cluster (8.3 kb) harbouring and ‐like genes was amplified from FAM5, sequenced and assembled. Two partial and six complete open reading frames arranged in the order were identified and subjected to mutational analysis, functional and metabolic profiling. We demonstrated that ‐like and ‐like genes play a key role in methylamine utilization and encode ‐methylglutamate synthetase and ‐methylglutamate dehydrogenase respectively. Metabolic, enzymatic and mutational analyses showed that the ‐like gene encodes γ‐glutamylmethylamide synthetase; however, this enzyme is not essential for oxidation of methylamine.
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subjectGenetic Research -- Analysis ; Genetic Research -- Genetic Aspects ; Biopolymers -- Analysis ; Biopolymers -- Genetic Aspects ; Enzymology -- Analysis ; Enzymology -- Genetic Aspects ; Glutamine -- Analysis ; Glutamine -- Genetic Aspects ; Glutamate -- Analysis ; Glutamate -- Genetic Aspects ; Oxidases -- Analysis ; Oxidases -- Genetic Aspects ; Polypeptides -- Analysis ; Polypeptides -- Genetic Aspects ; Ligases -- Analysis ; Ligases -- Genetic Aspects;
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titleGenetics of the glutamate‐mediated methylamine utilization pathway in the facultative methylotrophic beta‐proteobacterium Methyloversatilis universalis FAM5
descriptionThe ability of some microbial species to oxidize monomethylamine via glutamate‐mediated pathways was proposed in the 1960s; however, genetic determinants of the pathways have never been described. In the present study we describe a gene cluster essential for operation of the ‐methylglutamate pathway in the methylotrophic beta‐proteobacterium FAM5. Four major polypeptides from protein fractions displaying high activities of ‐methylglutamate synthetase, ‐methylglutamate dehydrogenase and γ‐glutamylmethylamide synthetase were selected for mass spectrometry‐based identification. The activities of enzymes were associated with the presence of peptides identified as ferredoxin‐dependent glutamate synthase (GltB2), large subunit of putative heterotetrameric sarcosine oxidase (SoxA) and glutamine synthetase type III (GSIII) respectively. A gene cluster (8.3 kb) harbouring and ‐like genes was amplified from FAM5, sequenced and assembled. Two partial and six complete open reading frames arranged in the order were identified and subjected to mutational analysis, functional and metabolic profiling. We demonstrated that ‐like and ‐like genes play a key role in methylamine utilization and encode ‐methylglutamate synthetase and ‐methylglutamate dehydrogenase respectively. Metabolic, enzymatic and mutational analyses showed that the ‐like gene encodes γ‐glutamylmethylamide synthetase; however, this enzyme is not essential for oxidation of methylamine.
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abstractThe ability of some microbial species to oxidize monomethylamine via glutamate‐mediated pathways was proposed in the 1960s; however, genetic determinants of the pathways have never been described. In the present study we describe a gene cluster essential for operation of the ‐methylglutamate pathway in the methylotrophic beta‐proteobacterium FAM5. Four major polypeptides from protein fractions displaying high activities of ‐methylglutamate synthetase, ‐methylglutamate dehydrogenase and γ‐glutamylmethylamide synthetase were selected for mass spectrometry‐based identification. The activities of enzymes were associated with the presence of peptides identified as ferredoxin‐dependent glutamate synthase (GltB2), large subunit of putative heterotetrameric sarcosine oxidase (SoxA) and glutamine synthetase type III (GSIII) respectively. A gene cluster (8.3 kb) harbouring and ‐like genes was amplified from FAM5, sequenced and assembled. Two partial and six complete open reading frames arranged in the order were identified and subjected to mutational analysis, functional and metabolic profiling. We demonstrated that ‐like and ‐like genes play a key role in methylamine utilization and encode ‐methylglutamate synthetase and ‐methylglutamate dehydrogenase respectively. Metabolic, enzymatic and mutational analyses showed that the ‐like gene encodes γ‐glutamylmethylamide synthetase; however, this enzyme is not essential for oxidation of methylamine.
copOxford, UK
pubBlackwell Publishing Ltd
doi10.1111/j.1365-2958.2009.06989.x
pages426-439
date2010-01