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Recently identified genes located downstream (3') of the msmEF (transport encoding) gene cluster, msmGH, and located 5' of the structural genes for methanesulfonate monooxygenase (MSAMO) are described from Methylosulfonomonas methylovora. Sequence analysis of the derived polypeptide sequences encoded by these genes revealed a high degree of identity to ABC-type transporters. MsmE showed similarity to a putative periplasmic substrate binding protein, MsmF resembled an integral membrane-associated protein, and MsmG was a putative ATP-binding enzyme. MsmH was thought to be the cognate permease component of the sulfonate transport system. The close association of these putative transport genes to the MSAMO structural genes msmABCD suggested a role for these genes in transport of methanesulfonic acid (MSA) into M. methylovora. msmEFGH and msmABCD constituted two operons for the coordinated expression of MSAMO and the MSA transporter systems. Reverse-transcription-PCR analysis of msmABCD and msmEFGH revealed differential expression of these genes during growth on MSA and methanol. The msmEFGH operon was constitutively expressed, whereas MSA induced expression of msmABCD. A mutant defective in msmE had considerably slower growth rates than the wild type, thus supporting the proposed role of MsmE in the transport of MSA into M. methylovora.
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http://dx.doi.org/10.1128/AEM.72.1.276-283.2006 | DOI Listing |
ISME J
March 2013
Plymouth Marine Laboratory, Plymouth, UK.
Methanol biogeochemistry and its importance as a carbon source in seawater is relatively unexplored. We report the first microbial methanol carbon assimilation rates (k) in productive coastal upwelling waters of up to 0.117±0.
View Article and Find Full Text PDFJ Basic Microbiol
September 2009
Cell and Applied Microbiology group, IBMC - Instituto de Biologia Celular e Celular, Universidade do Porto, R. Campo Alegre, 823, 4150-180, Porto, Portugal.
Methanesulfonate (MSA) is one of the products of the photo-oxidation of dimethylsulfide in the atmosphere. The genes responsible for the import of MSA into the cell (msm EFGH) and for its oxidation to formaldehyde (msm ABCD) have been previously sequenced from the soil bacterium Methylosulfonomonas methylovora str. M2 while genes for an MSA monooxygenase have been sequenced from marine bacterium Marinosulfonomonas methylotropha str.
View Article and Find Full Text PDFProtein Expr Purif
April 2007
Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK.
The aim of the work described in this paper was two-fold: (1) the purification of the hydroxylase component of the MSAMO to electrophoretic homogeneity using a four-step chromatographic strategy and (2) the crystallization of the two-component hydroxylase of the MSAMO in order to enhance our understanding of the precise three-dimensional structure of the MSAMO, thus yielding an insight into the nature of the active site of this enzyme. Optimised crystallization conditions were identified allowing growth of crystals of the hydroxylase component of the MSAMO within five days. Crystals exhibited a brown colour suggesting the presence on an intact Rieske-iron sulfur centre and diffracted to 7.
View Article and Find Full Text PDFAppl Environ Microbiol
January 2006
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom.
Recently identified genes located downstream (3') of the msmEF (transport encoding) gene cluster, msmGH, and located 5' of the structural genes for methanesulfonate monooxygenase (MSAMO) are described from Methylosulfonomonas methylovora. Sequence analysis of the derived polypeptide sequences encoded by these genes revealed a high degree of identity to ABC-type transporters. MsmE showed similarity to a putative periplasmic substrate binding protein, MsmF resembled an integral membrane-associated protein, and MsmG was a putative ATP-binding enzyme.
View Article and Find Full Text PDFAppl Environ Microbiol
January 2002
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom.
Marinosulfonomonas methylotropha strain TR3 is a marine methylotroph that uses methanesulfonic acid (MSA) as a sole carbon and energy source. The genes from M. methylotropha strain TR3 encoding methanesulfonate monooxygenase, the enzyme responsible for the initial oxidation of MSA to formaldehyde and sulfite, were cloned and sequenced.
View Article and Find Full Text PDF