THE METHANE MONOOXYGENASE GENE-CLUSTER OF METHYLOCOCCUS-CAPSULATUS (BATH)

被引:148
作者
STAINTHORPE, AC [1 ]
LEES, V [1 ]
SALMOND, GPC [1 ]
DALTON, H [1 ]
MURRELL, JC [1 ]
机构
[1] UNIV WARWICK,DEPT BIOL SCI,COVENTRY CV4 7AL,W MIDLANDS,ENGLAND
关键词
hemerythrin; iron-sulfur flavoprotein; methanotroph; nucleotide sequencing; Recombinant DNA; ribonucleotide reductase;
D O I
10.1016/0378-1119(90)90158-N
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Methane is oxidised to methanol in methanotrophic bacteria by the enzyme methane monooxygenase (MMO). Methylococcus capsulatus (Bath) produces a soluble MMO which oxidises a range of aliphatic and aromatic compounds with potential for commercial exploitation. This multicomponent enzyme has been extensively characterised and biochemical data have been used to identify a 12-kb fragment of Methylococcus DNA carrying the structural genes mmoY and mmoZ, coding for the β- and γ-subunits of MMO component A, the methane-binding protein. We now report the complete nucleotide (nt) sequence of mmoX, the gene encoding the α-subunit of component A which is found to be 5′ to mmoY and mmoZ. We also report the complete nt sequence of mmoC which encodes component C, the iron-sulfur flavoprotein of MMO, the N terminus of which is significantly homologous with spinach ferredoxin. The mmo structural genes are clustered within a 7-kb region and are closely linked to two small open reading frames of unknown function. © 1990.
引用
收藏
页码:27 / 34
页数:8
相关论文
共 35 条
[1]   RESTORATION OF PHENOTYPE IN ESCHERICHIA-COLI AUXOTROPHS BY PULB113-MEDIATED MOBILIZATION FROM METHYLOTROPHIC BACTERIA [J].
ALTAHO, NM ;
WARNER, PJ .
FEMS MICROBIOLOGY LETTERS, 1987, 43 (02) :235-239
[2]   NONHEME IRON PROTEINS .11. SOME GENETIC ASPECTS [J].
BENSON, AM ;
YASUNOBU, KT .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1969, 63 (04) :1269-&
[3]   PRIMARY STRUCTURE OF THE ESCHERICHIA-COLI RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE OPERON [J].
CARLSON, J ;
FUCHS, JA ;
MESSING, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (14) :4294-4297
[4]   RESOLUTION OF METHANE MONO-OXYGENASE OF METHYLOCOCCUS-CAPSULATUS-BATH INTO 3 COMPONENTS - PURIFICATION AND PROPERTIES OF COMPONENT-C, A-FLAVOPROTEIN [J].
COLBY, J ;
DALTON, H .
BIOCHEMICAL JOURNAL, 1978, 171 (02) :461-468
[5]  
COLLINS JF, 1987, NUCLEIC ACID PROTEIN, P323
[6]   EVIDENCE FOR A SPIN-COUPLED BINUCLEAR IRON UNIT AT THE ACTIVE-SITE OF THE PURPLE ACID-PHOSPHATASE FROM BEEF SPLEEN [J].
DAVIS, JC ;
AVERILL, BA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1982, 79 (15) :4623-4627
[7]   ALGINATE BIOSYNTHESIS - A MODEL SYSTEM FOR GENE-REGULATION AND FUNCTION IN PSEUDOMONAS [J].
DERETIC, V ;
GILL, JF ;
CHAKRABARTY, AM .
BIO-TECHNOLOGY, 1987, 5 (05) :469-+
[8]   THE XYLABC PROMOTER FROM THE PSEUDOMONAS-PUTIDA TOL PLASMID IS ACTIVATED BY NITROGEN REGULATORY GENES IN ESCHERICHIA-COLI [J].
DIXON, R .
MOLECULAR AND GENERAL GENETICS, 1986, 203 (01) :129-136
[9]   STRUCTURAL CHARACTERIZATION BY EXAFS SPECTROSCOPY OF THE BINUCLEAR IRON CENTER IN PROTEIN-A OF METHANE MONOOXYGENASE FROM METHYLOCOCCUS-CAPSULATUS (BATH) [J].
ERICSON, A ;
HEDMAN, B ;
HODGSON, KO ;
GREEN, J ;
DALTON, H ;
BENTSEN, JG ;
BEER, RH ;
LIPPARD, SJ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1988, 110 (07) :2330-2332
[10]  
GREEN J, 1985, J BIOL CHEM, V260, P5795