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Titolo:
HETEROLOGOUS EXPRESSION OF AN ENGINEERED BIOSYNTHETIC-PATHWAY - FUNCTIONAL DISSECTION OF TYPE-II POLYKETIDE SYNTHASE COMPONENTS IN STREPTOMYCES SPECIES
Autore:
KIM ES; CRAMER KD; SHREVE AL; SHERMAN DH;
Indirizzi:
UNIV MINNESOTA,INST BIOL PROC TECHNOL,1479 GORTNER AVE,NO 240 ST PAULMN 55108 UNIV MINNESOTA,INST BIOL PROC TECHNOL ST PAUL MN 55108 UNIV MINNESOTA,DEPT MICROBIOL ST PAUL MN 55108
Titolo Testata:
Journal of bacteriology
fascicolo: 5, volume: 177, anno: 1995,
pagine: 1202 - 1207
SICI:
0021-9193(1995)177:5<1202:HEOAEB>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
6-METHYLSALICYLIC ACID SYNTHASE; COELICOLOR A3(2); GENE-CLUSTER; ANTIBIOTIC ACTINORHODIN; PENICILLIUM-PATULUM; NUCLEOTIDE-SEQUENCE; MOLECULAR-CLONING; VIOLACEORUBER; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
E.S. Kim et al., "HETEROLOGOUS EXPRESSION OF AN ENGINEERED BIOSYNTHETIC-PATHWAY - FUNCTIONAL DISSECTION OF TYPE-II POLYKETIDE SYNTHASE COMPONENTS IN STREPTOMYCES SPECIES", Journal of bacteriology, 177(5), 1995, pp. 1202-1207

Abstract

Polyketides are an extensive class of secondary metabolites with diverse molecular structures and biological activities. A plasmid-based multicomponent polyketide synthase expression cassette was constructed using a subset of actinorhodin (act) biosynthetic genes (actI-orf1, actI-orf2, actI-orf3, actIII, actVII, and actIV) from Streptomyces coelicolor which specify the construction of the anthraquinone product aloesaponarin II, a molecule derived from acetyl coenzyme A and 7 malonyl coenzyme A extender units. This system was designed as an indicator pathway in Streptomyces parvulus to quantify polyketide product formationand to examine the functional significance of specific polyketide synthase components, including the act beta-ketoacyl synthase (beta-KS; encoded by actI-orf1 and actI-orf2) and the act cyclase/dehydrase (encoded by actVII-orf4). Site-directed mutagenesis of the putative active site Cys (to a Gin) in the actI-orf1 beta-KS product completely abrogated aloesaponarin II production. Changing the putative acyltransferaseactive-site Ser (to a Leu) located in the actI-orf1 beta-KS product led to significantly reduced but continued production of aloesaponarin II. Replacement of the expression cassette with one containing a mutant form of actI-orf2 gave no production of aloesaponarin LI or any other detectable polyketide products. However, an expression cassette containing a mutant form of actVII-orf4 gave primarily mutactin with low-level production of aloesaponarin II.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 01:18:13