The Library
Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5
Tools
Tools
Tools
Latypova, Ekaterina, Yang, Song, Wang, Yi-Shun, Wang, Tiansong, Chavkin, Theodore A., Hackett, Murray, Schaefer, Hendrik and Kalyuzhnaya, Marina G. (2010) Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5. Molecular Microbiology, Vol.75 (No.2). pp. 426-439. doi:10.1111/j.1365-2958.2009.06989.x ISSN 0950-382X.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/10.1111/j.1365-2958.2009.06989.x
Abstract
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 N-methylglutamate pathway in the methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5. Four major polypeptides from protein fractions displaying high activities of N-methylglutamate synthetase, N-methylglutamate dehydrogenase and g-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 gltB2, soxA and gsIII-like genes was amplified from M. universalis FAM5, sequenced and assembled. Two partial and six complete open reading frames arranged in the order soxBDAG-gsIII-gltB132 were identified and subjected to mutational analysis, functional and metabolic profiling. We demonstrated that gltB-like and sox-like genes play a key role in methylamine utilization and encode N-methylglutamate synthetase and N-methylglutamate dehydrogenase respectively. Metabolic, enzymatic and mutational analyses showed that the gsIII-like gene encodes g-glutamylmethylamide synthetase; however, this enzyme is not essential for oxidation of methylamine.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QR Microbiology |
||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Warwick HRI (2004-2010) | ||||
| Journal or Publication Title: | Molecular Microbiology | ||||
| Publisher: | Wiley-Blackwell Publishing Ltd. | ||||
| ISSN: | 0950-382X | ||||
| Official Date: | January 2010 | ||||
| Dates: |
|
||||
| Volume: | Vol.75 | ||||
| Number: | No.2 | ||||
| Number of Pages: | 14 | ||||
| Page Range: | pp. 426-439 | ||||
| DOI: | 10.1111/j.1365-2958.2009.06989.x | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Royalty Research Fund, National Science Foundation, NSF, NIGMS | ||||
| Grant number: | 65-1818, MCB-0842686, MCB-06044269, GM-58933 |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
