Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon Methanococcus maripaludis
Abstract
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.
- Publication Date:
- Research Org.:
- Univ. of Georgia, Athens, GA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); Natural Science Foundation of Jiangsu Province
- OSTI Identifier:
- 1595760
- Grant/Contract Number:
- SC0018028; BK20171266
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of Bacteriology
- Additional Journal Information:
- Journal Volume: 200; Journal Issue: 7; Journal ID: ISSN 0021-9193
- Publisher:
- American Society for Microbiology
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 03 NATURAL GAS; 09 BIOMASS FUELS; 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; coenzyme F430; methyl coenzyme M reductase; posttranslational modification; Methanococcus; Methanothermococcus
Citation Formats
Lyu, Zhe, Chou, Chau-Wen, Shi, Hao, Wang, Liangliang, Ghebreab, Robel, Phillips, Dennis, Yan, Yajun, Duin, Evert C., and Whitman, William B. Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon Methanococcus maripaludis. United States: N. p., 2018.
Web. doi:10.1128/JB.00746-17.
Lyu, Zhe, Chou, Chau-Wen, Shi, Hao, Wang, Liangliang, Ghebreab, Robel, Phillips, Dennis, Yan, Yajun, Duin, Evert C., & Whitman, William B. Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon Methanococcus maripaludis. United States. https://doi.org/10.1128/JB.00746-17
Lyu, Zhe, Chou, Chau-Wen, Shi, Hao, Wang, Liangliang, Ghebreab, Robel, Phillips, Dennis, Yan, Yajun, Duin, Evert C., and Whitman, William B. Tue .
"Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon Methanococcus maripaludis". United States. https://doi.org/10.1128/JB.00746-17. https://www.osti.gov/servlets/purl/1595760.
@article{osti_1595760,
title = {Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon Methanococcus maripaludis},
author = {Lyu, Zhe and Chou, Chau-Wen and Shi, Hao and Wang, Liangliang and Ghebreab, Robel and Phillips, Dennis and Yan, Yajun and Duin, Evert C. and Whitman, William B.},
abstractNote = {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.},
doi = {10.1128/JB.00746-17},
journal = {Journal of Bacteriology},
number = 7,
volume = 200,
place = {United States},
year = {Tue Jan 16 00:00:00 EST 2018},
month = {Tue Jan 16 00:00:00 EST 2018}
}
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