Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A 3-(3-HYDROXYPHENYL)PROPIONIC ACID CATABOLIC PATHWAY IN RHODOCOCCUS-GLOBERULUS PWD1 - CLONING AND CHARACTERIZATION OF THE HPP OPERON
Autore:
BARNES MR; DUETZ WA; WILLIAMS PA;
Indirizzi:
UNIV COLL N WALES,SCH BIOL SCI BANGOR LL57 2UW GWYNEDD WALES UNIV COLL N WALES,SCH BIOL SCI BANGOR LL57 2UW GWYNEDD WALES NATL INST PUBL HLTH & ENVIRONM,LAB ECOTOXICOL NL-3720 BA BILTHOVEN NETHERLANDS
Titolo Testata:
Journal of bacteriology
fascicolo: 19, volume: 179, anno: 1997,
pagine: 6145 - 6153
SICI:
0021-9193(1997)179:19<6145:A3ACPI>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOMONAS-PUTIDA F1; ESCHERICHIA-COLI; ACINETOBACTER-CALCOACETICUS; TRANSCRIPTIONAL ACTIVATOR; EVOLUTIONARY DIVERGENCE; SEQUENCE-ANALYSIS; GENE-CLUSTER; SEARCH TOOL; DEGRADATION; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
M.R. Barnes et al., "A 3-(3-HYDROXYPHENYL)PROPIONIC ACID CATABOLIC PATHWAY IN RHODOCOCCUS-GLOBERULUS PWD1 - CLONING AND CHARACTERIZATION OF THE HPP OPERON", Journal of bacteriology, 179(19), 1997, pp. 6145-6153

Abstract

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 orsuccinate, 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), anextradiol 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 deducedamino 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 14:18:36