دورية أكاديمية

Metabolism of Poly(3-hydroxyalkanoates) (PHAs) by Pseudomonas oleovorans. Identification and Sequences of Genes and Function of the Encoded Proteins in the Synthesis and Degradation of PHA

التفاصيل البيبلوغرافية
العنوان: Metabolism of Poly(3-hydroxyalkanoates) (PHAs) by Pseudomonas oleovorans. Identification and Sequences of Genes and Function of the Encoded Proteins in the Synthesis and Degradation of PHA
المؤلفون: Huisman, Gjalt W., Wonink, Eric, Meima, Rob, Kazemier, Bert, Terpstra, Peter, Witholt, Bernard
المصدر: Huisman , G W , Wonink , E , Meima , R , Kazemier , B , Terpstra , P & Witholt , B 1991 , ' Metabolism of Poly(3-hydroxyalkanoates) (PHAs) by Pseudomonas oleovorans. Identification and Sequences of Genes and Function of the Encoded Proteins in the Synthesis and Degradation of PHA ' , The Journal of Biological Chemistry , vol. 266 , no. 4 , pp. 2191-2198 .
سنة النشر: 1991
المجموعة: University of Groningen research database
مصطلحات موضوعية: POLY-BETA-HYDROXYBUTYRATE, ALCALIGENES-EUTROPHUS H16, BROAD HOST RANGE, ACETOACETYL-COA REDUCTASE, ESCHERICHIA-COLI, NUCLEOTIDE-SEQUENCE, ALKALINE EXTRACTION, ZOOGLOEA-RAMIGERA, COSMID CLONING, DNA
الوصف: Pseudomonas oleovorans accumulates poly(3-hydroxyalkanoates) (PHAs) after growth on medium chain length hydrocarbons. Large amounts of this polyester are synthesized when cells are grown under nitrogen-limiting conditions. When nitrogen is resupplied in the medium, the accumulated PHA is degraded. In this paper, we describe mutants which are defective in the synthesis or in the degradation of PHA. These mutants were used to select DNA fragments which encode PHA polymerases and a PHA depolymerase. A 25-kilobase (kb) DNA fragment was isolated from P. oleovorans that complements a Pseudomonas putida mutant unable to accumulate PHA. Subcloning resulted in the assignment of a 6.4-kb EcoRI fragment as the pha locus, containing genetic information of PHA synthesis. Mutants in the PHA degradation pathway were also complemented by this fragment, indicating that genes encoding PHA biosynthetic and degradative enzymes are clustered. Analysis of the DNA sequence of the 6.4-kb fragment revealed the presence of two open reading frames encoding PHA polymerases based on homology to the poly(3-hydroxybutyrate) polymerase from Alcaligenes eutrophus. A third open reading frame complemented the PHA degradation mutation and is likely to encode a PHA depolymerase. The presence of two PHA polymerases is due to a 2098-base pair DNA duplication. The PHA polymerases are 53% identical and show 35-40% identity to the poly(3-hydroxybutyrate) polymerase. No clear difference in specificity was found for the PHA polymerases. However, with the pha locus cloned on a multicopy vector, a polymer was accumulated that contains a significantly higher amount of substrate-derived monomers. An increase in the rate of polyester synthesis versus oxidation of the monomers in the beta-oxidation explains these findings.
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
العلاقة: https://research.rug.nl/en/publications/988ef9ed-fc7b-49cf-a862-5afb273a5e0bTest
الإتاحة: https://hdl.handle.net/11370/988ef9ed-fc7b-49cf-a862-5afb273a5e0bTest
https://research.rug.nl/en/publications/988ef9ed-fc7b-49cf-a862-5afb273a5e0bTest
https://pure.rug.nl/ws/files/37044617/1991JBiolChemHuisman.pdfTest
حقوق: info:eu-repo/semantics/openAccess
رقم الانضمام: edsbas.EC9629B7
قاعدة البيانات: BASE