The Genetic Basis for Bacterial Mercury Methylation

被引:758
作者
Parks, Jerry M. [1 ]
Johs, Alexander [2 ]
Podar, Mircea [1 ,3 ]
Bridou, Romain [4 ]
Hurt, Richard A., Jr. [1 ]
Smith, Steven D. [4 ]
Tomanicek, Stephen J. [2 ]
Qian, Yun [2 ]
Brown, Steven D. [1 ,5 ]
Brandt, Craig C. [1 ]
Palumbo, Anthony V. [1 ]
Smith, Jeremy C. [1 ,5 ]
Wall, Judy D. [4 ]
Elias, Dwayne A. [1 ,5 ]
Liang, Liyuan [2 ]
机构
[1] Oak Ridge Natl Lab, Biosci Div, Oak Ridge, TN 37831 USA
[2] Oak Ridge Natl Lab, Div Environm Sci, Oak Ridge, TN 37831 USA
[3] Univ Tennessee, Dept Microbiol, Knoxville, TN 37996 USA
[4] Univ Missouri, Div Biochem, Columbia, MO 65211 USA
[5] Univ Tennessee, Dept Biochem & Cellular & Mol Biol, Knoxville, TN 37996 USA
关键词
SP NOV; PRINCIPAL METHYLATORS; REDUCING BACTERIA; ACETYL-COENZYME; GEN; NOV; SULFATE; METHYLTETRAHYDROFOLATE; PATHWAYS; ELECTRON; ACETATE;
D O I
10.1126/science.1230667
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Methylmercury is a potent neurotoxin produced in natural environments from inorganic mercury by anaerobic bacteria. However, until now the genes and proteins involved have remained unidentified. Here, we report a two-gene cluster, hgcA and hgcB, required for mercury methylation by Desulfovibrio desulfuricans ND132 and Geobacter sulfurreducens PCA. In either bacterium, deletion of hgcA, hgcB, or both genes abolishes mercury methylation. The genes encode a putative corrinoid protein, HgcA, and a 2[4Fe-4S] ferredoxin, HgcB, consistent with roles as a methyl carrier and an electron donor required for corrinoid cofactor reduction, respectively. Among bacteria and archaea with sequenced genomes, gene orthologs are present in confirmed methylators but absent in nonmethylators, suggesting a common mercury methylation pathway in all methylating bacteria and archaea sequenced to date.
引用
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页码:1332 / 1335
页数:4
相关论文
共 31 条
[1]  
Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkp985, 10.1093/nar/gkh121, 10.1093/nar/gkr1065]
[2]   Genome Sequence of the Mercury-Methylating Strain Desulfovibrio desulfuricans ND132 [J].
Brown, Steven D. ;
Gilmour, Cynthia C. ;
Kucken, Amy M. ;
Wall, Judy D. ;
Elias, Dwayne A. ;
Brandt, Craig C. ;
Podar, Mircea ;
Chertkov, Olga ;
Held, Brittany ;
Bruce, David C. ;
Detter, John C. ;
Tapia, Roxanne ;
Han, Cliff S. ;
Goodwin, Lynne A. ;
Cheng, Jan-Fang ;
Pitluck, Samuel ;
Woyke, Tanja ;
Mikhailova, Natalia ;
Ivanova, Natalia N. ;
Han, James ;
Lucas, Susan ;
Lapidus, Alla L. ;
Land, Miriam L. ;
Hauser, Loren J. ;
Palumbo, Anthony V. .
JOURNAL OF BACTERIOLOGY, 2011, 193 (08) :2078-2079
[3]   Sequestration of Hg2+ by Some Biologically Important Thiols [J].
Cardiano, Paola ;
Falcone, Gabriella ;
Foti, Claudia ;
Sammartano, Silvio .
JOURNAL OF CHEMICAL AND ENGINEERING DATA, 2011, 56 (12) :4741-4750
[4]   ENZYMATIC CATALYSIS OF MERCURY METHYLATION BY DESULFOVIBRIO-DESULFURICANS LS [J].
CHOI, SC ;
CHASE, T ;
BARTHA, R .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1994, 60 (04) :1342-1346
[5]   METABOLIC PATHWAYS LEADING TO MERCURY METHYLATION IN DESULFOVIBRIO-DESULFURICANS LS [J].
CHOI, SC ;
CHASE, T ;
BARTHA, R .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1994, 60 (11) :4072-4077
[6]   SULFATE-REDUCING BACTERIA - PRINCIPAL METHYLATORS OF MERCURY IN ANOXIC ESTUARINE SEDIMENT [J].
COMPEAU, GC ;
BARTHA, R .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1985, 50 (02) :498-502
[7]   KINETICS AND MECHANISM OF COBALAMIN-DEPENDENT METHYL AND ETHYL TRANSFER TO MERCURIC ION [J].
DESIMONE, RE ;
PENLEY, MW ;
CHARBONNEAU, L ;
SMITH, SG ;
WOOD, JM ;
HILL, HAO ;
PRATT, JM ;
RIDSDALE, S ;
WILLIAMS, RJP .
BIOCHIMICA ET BIOPHYSICA ACTA, 1973, 304 (03) :851-863
[8]   Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase [J].
Doukov, T ;
Seravalli, J ;
Stezowski, JJ ;
Ragsdale, SV .
STRUCTURE, 2000, 8 (08) :817-830
[9]   A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase [J].
Doukov, TI ;
Iverson, TM ;
Seravalli, J ;
Ragsdale, SW ;
Drennan, CL .
SCIENCE, 2002, 298 (5593) :567-572
[10]  
DRAKE HL, 1981, J BIOL CHEM, V256, P1137