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Titolo:
Characterization of an extracellular lipase encoded by LIP2 in Yarrowia lipolytica
Autore:
Pignede, G; Wang, HJ; Fudalej, F; Gaillardin, C; Seman, M; Nicaud, JM;
Indirizzi:
INRA, Lab Microbiol & Genet Mol, Grignon CNRS, F-78850 Thiverval Grignon, France INRA Thiverval Grignon France F-78850 F-78850 Thiverval Grignon, France Lab Mayoly Spindler, Serv Rech, F-78401 Chatou, France Lab Mayoly Spindler Chatou France F-78401 v Rech, F-78401 Chatou, France
Titolo Testata:
JOURNAL OF BACTERIOLOGY
fascicolo: 10, volume: 182, anno: 2000,
pagine: 2802 - 2810
SICI:
0021-9193(200005)182:10<2802:COAELE>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
CANDIDA-RUGOSA LIPASES; SACCHAROMYCOPSIS-LIPOLYTICA; NUCLEOTIDE-SEQUENCE; GENE DISRUPTION; YEAST; PROTEASE; CLONING; SITES; SECRETION; PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Nicaud, JM INRA, Lab Microbiol & Genet Mol, Grignon CNRS, BP 01, F-78850 Thiverval Grignon, France INRA BP 01 Thiverval Grignon France F-78850 al Grignon, France
Citazione:
G. Pignede et al., "Characterization of an extracellular lipase encoded by LIP2 in Yarrowia lipolytica", J BACT, 182(10), 2000, pp. 2802-2810

Abstract

We isolated the LIP2 gene from the lipolytic yeast Yarrowia lipolytica. Itwas found to encode a 334-amino-acid precursor protein. The secreted lipase is a 301-amino-acid glycosylated polypeptide which is a member of the triacylglycerol hydrolase family (EC 3.1.1.3). The Lip2p precursor protein is processed by the KEX2-like endoprotease encoded by XPR6. Deletion of the XPR6 gene resulted in the secretion of an active but less stable proenzyme. Thus, the pro region does not inhibit lipase secretion and activity. However, it does play an essential role in the production of a stable enzyme. Processing was found to he correct in LIP2(A) (multiple LIP2 copy integrant)-overexpressing strains, which secreted 100 times more activity than the wild type, demonstrating that XPR6 maturation was not limiting. No extracellularlipase activity was detected with the lip2 knockout (KO) strain, strongly suggesting that extracellular lipase activity results from expression of the LIP2 gene. Nevertheless, the lip2 KO strain is still able to grow on triglycerides, suggesting an alternative pathway for triglyceride utilization in Y. lipolytica.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 09:55:20