A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: Cloning and characterization of the hpp operon

被引:35
作者
Barnes, MR
Duetz, WA
Williams, PA
机构
[1] UNIV COLL N WALES,SCH BIOL SCI,BANGOR LL57 2UW,GWYNEDD,WALES
[2] NATL INST PUBL HLTH & ENVIRONM,LAB ECOTOXICOL,NL-3720 BA BILTHOVEN,NETHERLANDS
关键词
D O I
10.1128/jb.179.19.6145-6153.1997
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Rhodococcus globerulus PWD1, a soil isolate from a polluted site in The Netherlands, is able to degrade a broad range of aromatic compounds, A novel gene cluster which appears to encode a pathway for the degradation of phenolic acids such as 3-(3-hydroxyphenyl) propionate (3HPP) has been cloned from the chromosome of this organism, Sequence analysis of a 7-kb region identified five open reading frames (ORFs), Analysis of mRNA showed that the genes were expressed during growth on 3HPP and 3-hydroxyphenylacetate (3HPA) but not during growth on m-cresol or succinate, The first ORF, hppA, which appears to be separately transcribed, had considerable amino acid identity with a number of hydroxylases. Transcriptional analysis indicates that the next four ORFs, hppCBKR, which are tightly clustered, constitute a single operon, These genes appear to encode a hydroxymuconic semialdehyde hydrolase (HppC), an extradiol dioxygenase (HppB), a membrane transport protein (HppK), and a member of the IcIR family of regulatory proteins (HppR), The activities of HppB and HppC have been confirmed by enzyme assay of Escherichia coli hosts, The substrate specificity of HppB expressed from the cloned gene matches that of the meta-cleavage dioxygenase expressed from wild-type Rhodococcus grown on both 3HPP and 3HPA and is considerably more active against acid than against neutral catechols, The deduced amino acid sequences of the gene products have a recognizable homology with a broad range of enzymes and proteins involved in biodegradation and appear most similar to the mhp operon from E. coli K-12, which also encodes the degradation of 3HPP.
引用
收藏
页码:6145 / 6153
页数:9
相关论文
共 56 条
[21]   NUCLEOTIDE-SEQUENCE OF METAPYROCATECHASE-I (CATECHOL 2,3-OXYGENASE-I) GENE MPCL FROM ALCALIGENES-EUTROPHUS JMP222 [J].
KABISCH, M ;
FORTNAGEL, P .
NUCLEIC ACIDS RESEARCH, 1990, 18 (11) :3405-3405
[22]  
KAPLANA GV, 1991, P NATL ACAD SCI USA, V88, P5433
[23]  
KAWAMUKAI M, 1996, UNPUB
[24]   CONTRASTING PATTERNS OF EVOLUTIONARY DIVERGENCE WITHIN THE ACINETOBACTER-CALCOACETICUS PCA OPERON [J].
KOWALCHUK, GA ;
HARTNETT, GB ;
BENSON, A ;
HOUGHTON, JE ;
NGAI, KL ;
ORNSTON, LN .
GENE, 1994, 146 (01) :23-30
[25]   A SIMPLE METHOD FOR DISPLAYING THE HYDROPATHIC CHARACTER OF A PROTEIN [J].
KYTE, J ;
DOOLITTLE, RF .
JOURNAL OF MOLECULAR BIOLOGY, 1982, 157 (01) :105-132
[26]   The tfdR gene product can successfully take over the role of the insertion element-inactivated TfdT protein as a transcriptional activator of the tfdCDEF gene cluster, which encodes chlorocatechol degradation in Ralstonia eutropha JMP134(pJP4) [J].
Leveau, JHJ ;
vanderMeer, JR .
JOURNAL OF BACTERIOLOGY, 1996, 178 (23) :6824-6832
[27]  
LEVY CC, 1967, J BIOL CHEM, V242, P747
[28]   A MAJOR SUPERFAMILY OF TRANSMEMBRANE FACILITATORS THAT CATALYZE UNIPORT, SYMPORT AND ANTIPORT [J].
MARGER, MD ;
SAIER, MH .
TRENDS IN BIOCHEMICAL SCIENCES, 1993, 18 (01) :13-20
[29]   PROCEDURE FOR ISOLATION OF DEOXYRIBONUCLEIC ACID FROM MICRO-ORGANISMS [J].
MARMUR, J .
JOURNAL OF MOLECULAR BIOLOGY, 1961, 3 (02) :208-&
[30]   LOCATION AND SEQUENCE OF THE TODF GENE ENCODING 2-HYDROXY-6-OXOHEPTA-2,4-DIENOATE HYDROLASE IN PSEUDOMONAS-PUTIDA F1 [J].
MENN, FM ;
ZYLSTRA, GJ ;
GIBSON, DT .
GENE, 1991, 104 (01) :91-94