Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon Methanococcus maripaludis
- Univ. of Georgia, Athens, GA (United States)
- Auburn Univ., AL (United States)
Methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. To better understand its assembly, the recombinant MCR from the thermophile Methanothermococcus okinawensis (rMCRok) was expressed in the mesophile Methanococcus maripaludis. The rMCRok was posttranslationally modified correctly and contained McrD and the unique nickel tetrapyrrole coenzyme F430. Subunits of the native M. maripaludis (MCRmar) were largely absent, suggesting that the recombinant enzyme was formed by an assembly of cotranscribed subunits. Strong support for this hypothesis was obtained by expressing a chimeric operon comprising the His-tagged mcrA from M. maripaludis and the mcrBDCG from M. okinawensis in M. maripaludis. The His-tagged purified rMCR then contained the M. maripaludis McrA and the M. okinawensis McrBDG. The present study prompted us to form a working model for MCR assembly, which can be further tested by the heterologous expression system established here.
- Research Organization:
- Univ. of Georgia, Athens, GA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); Natural Science Foundation of Jiangsu Province
- Grant/Contract Number:
- SC0018028; BK20171266
- OSTI ID:
- 1595760
- Journal Information:
- Journal of Bacteriology, Vol. 200, Issue 7; ISSN 0021-9193
- Publisher:
- American Society for MicrobiologyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
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