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Four families of folate-independent methionine synthases


Autoři: Morgan N. Price aff001;  Adam M. Deutschbauer aff001;  Adam P. Arkin aff001
Působiště autorů: Environmental Genomics and Systems Biology, Lawrence Berkeley National Lab, Berkeley, California, United States of America aff001;  Department of Bioengineering, University of California, Berkeley, California, United States of America aff002
Vyšlo v časopise: Four families of folate-independent methionine synthases. PLoS Genet 17(2): e1009342. doi:10.1371/journal.pgen.1009342
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.pgen.1009342

Souhrn

Although most organisms synthesize methionine from homocysteine and methyl folates, some have “core” methionine synthases that lack folate-binding domains and use other methyl donors. In vitro, the characterized core synthases use methylcobalamin as a methyl donor, but in vivo, they probably rely on corrinoid (vitamin B12-binding) proteins. We identified four families of core methionine synthases that are distantly related to each other (under 30% pairwise amino acid identity). From the characterized enzymes, we identified the families MesA, which is found in methanogens, and MesB, which is found in anaerobic bacteria and archaea with the Wood-Ljungdahl pathway. A third uncharacterized family, MesC, is found in anaerobic archaea that have the Wood-Ljungdahl pathway and lack known forms of methionine synthase. We predict that most members of the MesB and MesC families accept methyl groups from the iron-sulfur corrinoid protein of that pathway. The fourth family, MesD, is found only in aerobic bacteria. Using transposon mutants and complementation, we show that MesD does not require 5-methyltetrahydrofolate or cobalamin. Instead, MesD requires an uncharacterized protein family (DUF1852) and oxygen for activity.

Klíčová slova:

Archaea – Cobalamins – Genomics – Methanogens – Methionine – Phylogenetic analysis – Protein domains – Proteomes


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