Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon <em>Methanococcus maripaludis</em> [electronic resource]

• Ngôn ngữ: eng
• Ký hiệu phân loại: 668.5 Perfumes and cosmetics
• Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2018
• Mô tả vật lý: Size: Article No. e00746-17 : , digital, PDF file.
• Bộ sưu tập: Metadata
• ID: 263098
• Chủ đề: 1. 03 natural gas; 2. 09 biomass fuels; 3. 59 basic biological sciences; 4. 60 applied life sciences; 5. Coenzyme f430

Tóm tắt

 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 F<
 sub>
 430<
 /sub>
 . 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.