Genetic and proteomic analyses of CO utilization by Methanosarcina acetivorans

被引:39
作者
Rother, Michael
Oelgeschlaeger, Ellen
Metcalf, William W.
机构
[1] Univ Illinois, Dept Microbiol, Urbana, IL 61801 USA
[2] Goethe Univ Frankfurt, Abt Mol Mikrobiol & Bioengn, Inst Mol Biowissenschaft, D-60438 Frankfurt, Germany
关键词
Methanosarcina acetivorans; carbon monoxide; carbon monoxide dehydrogenase;
D O I
10.1007/s00203-007-0266-1
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Methanosarcina acetivorans, a member of the methanogenic archaea, can grow with carbon monoxide (CO) as the sole energy source and generates, unlike other methanogens, substantial amounts of acetate and formate in addition to methane. Phenotypic analyses of mutant strains lacking the cooS1F operon and the cooS2 gene suggest that the monofunctional carbon monoxide dehydrogenase (CODH) system contributes to, but is not required for, carboxidotrophic growth of M. acetivorans. Further, qualitative proteomic analyses confirm a recent report (Lessner et al., Proc Natl Acad Sci USA, 103:17921-17926, 2006) in showing that the bifunctional CODH/acetyl-CoA synthase (ACS) system, two enzymes involved in CO2-reduction, and a peculiar protein homologous to both corrinoid proteins and methyltransferases are synthesized at elevated levels in response to CO; however, the finding that the latter protein is also abundant when trimethylamine serves as growth substrate questions its proposed involvement in the reduction of methyl-groups to methane. Potential catabolic mechanisms and metabolic adaptations employed by M. acetivorans to effectively utilize CO are discussed.
引用
收藏
页码:463 / 472
页数:10
相关论文
共 47 条
[1]   RESOLUTION OF COMPONENT PROTEINS IN AN ENZYME COMPLEX FROM METHANOSARCINA-THERMOPHILA CATALYZING THE SYNTHESIS OR CLEAVAGE OF ACETYL-COA [J].
ABBANAT, DR ;
FERRY, JG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (08) :3272-3276
[2]  
Ausubel F.A., 1997, CURRENT PROTOCOLS MO, DOI DOI 10.1.4
[3]   Generation of dominant selectable markers for resistance to pseudomonic acid by cloning and mutagenesis of the ileS gene from the archaeon Methanosarcina barkeri Fusaro [J].
Boccazzi, P ;
Zang, JK ;
Metcalf, WW .
JOURNAL OF BACTERIOLOGY, 2000, 182 (09) :2611-2618
[4]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[5]   Reconstitution of monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri [J].
Burke, SA ;
Krzycki, JA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (26) :16570-16577
[6]   Final steps in the catabolism of nicotine -: Deamination versus demethylation of γ-N-methylaminobutyrate [J].
Chiribau, CB ;
Mihasan, M ;
Ganas, P ;
Igloi, GL ;
Artenie, V ;
Brandsch, R .
FEBS JOURNAL, 2006, 273 (07) :1528-1536
[7]   Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS MS and database searching [J].
Clauser, KR ;
Baker, P ;
Burlingame, AL .
ANALYTICAL CHEMISTRY, 1999, 71 (14) :2871-2882
[8]   CARBON-MONOXIDE OXIDATION BY METHANOGENIC BACTERIA [J].
DANIELS, L ;
FUCHS, G ;
THAUER, RK ;
ZEIKUS, JG .
JOURNAL OF BACTERIOLOGY, 1977, 132 (01) :118-126
[9]  
Deppenmeier U, 2002, J MOL MICROB BIOTECH, V4, P453
[10]   Carbon monoxide dehydrogenase from Methanosarcina frisia Go1 - Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters [J].
Eggen, RIL ;
vanKranenburg, R ;
Vriesema, AJM ;
Geerling, ACM ;
Verhagen, MFJM ;
Hagen, WR ;
deVos, WM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (24) :14256-14263