title: Connection between multimetal(loid) methylation in methanoarchaea and central intermediates of methanogenesis.
abstract: In spite of the significant impact of biomethylation on the mobility and toxicity of metals and metalloids in the environment, little is known about the biological formation of these methylated metal(loid) compounds. While element-specific methyltransferases have been isolated for arsenic, the striking versatility of methanoarchaea to methylate numerous metal(loid)s, including rare elements like bismuth, is still not understood. Here, we demonstrate that the same metal(loid)s (arsenic, selenium, antimony, tellurium, and bismuth) that are methylated by Methanosarcina mazei in vivo are also methylated by in vitro assays with purified recombinant MtaA, a methyltransferase catalyzing the methyl transfer from methylcobalamin [CH₃Cob(III)] to 2-mercaptoethanesulfonic acid (CoM) in methylotrophic methanogenesis. Detailed studies revealed that cob(I)alamin [Cob(I)], formed by MtaA-catalyzed demethylation of CH₃Cob(III), is the causative agent for the multimetal(loid) methylation observed. Moreover, Cob(I) is also capable of metal(loid) hydride generation. Global transcriptome profiling of M. mazei cultures exposed to bismuth did not reveal induced methyltransferase systems but upregulated regeneration of methanogenic cofactors in the presence of bismuth. Thus, we conclude that the multimetal(loid) methylation in vivo is attributed to side reactions of CH₃Cob(III) with reduced cofactors formed in methanogenesis. The close connection between metal(loid) methylation and methanogenesis explains the general capability of methanoarchaea to methylate metal(loid)s.
authors: Department of Microbiology I, University of Duisburg-Essen, Campus Essen, Universitaetsstr. 2, 45141 Essen, Germany. frank.thomas@uni-due.de
authors: Frank
authors: F
authors: Thomas
authors: Roland A
authors: RA
authors: Diaz-Bone
authors: Oliver
authors: O
authors: Wuerfel
authors: Britta
authors: B
authors: Huber
authors: Katrin
authors: K
authors: Weidenbach
authors: Ruth A
authors: RA
authors: Schmitz
authors: Reinhard
authors: R
authors: Hensel
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D015080:Mesna / Q000378:metabolism; D008670:Metals / Q000378:metabolism*; D017020:Methanosarcina / Q000378:metabolism*; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D014805:Vitamin B 12 / Q000031:analogs & derivatives / Q000378:metabolism
chemical_list: D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D008670:Metals; C112062:Mta72 protein, bacteria; D011994:Recombinant Proteins; C019476:mecobalamin; D008780:Methyltransferases; D015080:Mesna; D014805:Vitamin B 12