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In vivo role of three fused corrinoid/methyl transfer proteins in Methanosarcina acetivorans.
- Source :
-
Molecular microbiology [Mol Microbiol] 2009 Jun; Vol. 72 (5), pp. 1260-72. Date of Electronic Publication: 2009 Apr 30. - Publication Year :
- 2009
-
Abstract
- Methanosarcina acetivorans is able to use carbon monoxide (CO) as the sole source of energy for growth. Its carboxidotrophic growth is peculiar as it involves formation of acetate, formate and methylated thiols, besides methane. Under this condition three proteins homologous to both corrinoid proteins and methyltransferases (MA0859, MA4384 and MA4558) are highly abundant. To address their role in M. acetivorans, a set of single and double mutants, and the triple mutant, was constructed by deletion/disruption of the encoding genes. Phenotypic analysis of the mutants rules out an important role of the methyltransferase homologues in the CO(2) reduction pathway of methanogenesis. Instead, the single and double mutants were affected to various degrees in their capacity to generate dimethylsulphide (DMS) from CO and to form methane from DMS. The triple mutant was unable to produce or metabolize DMS, and could not grow with DMS as the sole energy source, which demonstrates that MA0859, MA4384 and MA4558 are involved in, and required for, methylsulphide metabolism of M. acetivorans. Based on these findings we propose to designate MA0859, MA4384 and MA4558 as methyltransferases specific for methylsulphides, MtsD, MtsF and MtsH respectively.
- Subjects :
- Archaeal Proteins genetics
Carbon Monoxide metabolism
DNA, Archaeal genetics
Methane metabolism
Methanosarcina metabolism
Methyltransferases genetics
Mutation
Substrate Specificity
Sulfides metabolism
Archaeal Proteins metabolism
Corrinoids metabolism
Methanosarcina genetics
Methyltransferases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1365-2958
- Volume :
- 72
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Molecular microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 19432805
- Full Text :
- https://doi.org/10.1111/j.1365-2958.2009.06723.x