Computational analysis of cysteine and methionine metabolism and its regulation in dairy starter and related bacteria.
Publication year
2012Source
Journal of Bacteriology, 194, 13, (2012), pp. 3522-33ISSN
Annotation
01 juli 2012
Publication type
Article / Letter to editor

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Organization
CMBI
Journal title
Journal of Bacteriology
Volume
vol. 194
Issue
iss. 13
Page start
p. 3522
Page end
p. 33
Subject
NCMLS 4: Energy and redox metabolismAbstract
Sulfuric volatile compounds derived from cysteine and methionine provide many dairy products with a characteristic odor and taste. To better understand and control the environmental dependencies of sulfuric volatile compound formation by the dairy starter bacteria, we have used the available genome sequence and experimental information to systematically evaluate the presence of the key enzymes and to reconstruct the general modes of transcription regulation for the corresponding genes. The genomic organization of the key genes is suggestive of a subdivision of the reaction network into five modules, where we observed distinct differences in the modular composition between the families Lactobacillaceae, Enterococcaceae, and Leuconostocaceae, on the one hand, and the family Streptococcaceae, on the other. These differences are mirrored by the way in which transcription regulation of the genes is structured in these families. In the Lactobacillaceae, Enterococcaceae, and Leuconostocaceae, the main shared mode of transcription regulation is methionine (Met) T-box-mediated regulation. In addition, the gene metK, encoding S-adenosylmethionine (SAM) synthetase, is controlled via the S(MK) box (SAM). The S(MK) box is also found upstream of metK in species of the family Streptococcaceae. However, the transcription control of the other modules is mediated via three different LysR-family regulators, MetR/MtaR (methionine), CmbR (O-acetyl[homo]serine), and HomR (O-acetylhomoserine). Redefinition of the associated DNA-binding motifs helped to identify/disentangle the related regulons, which appeared to perfectly match the proposed subdivision of the reaction network.
This item appears in the following Collection(s)
- Academic publications [227245]
- Faculty of Medical Sciences [86731]
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