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Title 

Mutation of the protein-O-mannosyltransferase enhances secretion of the human urokinase-type plasminogen activator in Hansenula polymorpha

Authors 

M O AgaphonovS S SokolovN V RomanovaJung Hoon SohnSo Young KimT S KalebinaEui Sung ChoiM D Ter-Avanesyan

Publisher 

Wiley-Blackwell

Issue Date 

2005

Citation 

Yeast, vol. 22, no. 13, pp. 1037-1047

Keywords 

endoplasmic reticulumhansenula polymorphao-mannosylationprotein foldingprotein glycosylationprotein secretionmannosyltransferasemembrane proteinurokinasecarboxy terminal sequence

Abstract 

Human urokinase-type plasminogen activator (uPA) is poorly secreted and aggregates in the endoplasmic reticulum of yeast cells due to inefficient folding. A screen for Hansenula polymorpha mutants with improved uPA secretion revealed a gene encoding a homologue of the Saccharomyces cerevisiae protein-O-mannosyltransferase Pmt1p. Expression of the H. polymorpha PMT1 gene (HpPMT1) abolished temperature sensitivity of the S. cerevisiae pmt1 pmt2 double mutant. As in S. cerevisiae, inactivation of the HpPMT1 gene affected electrophoretic mobility of the O-glycosylated protein, extracellular chitinase. In contrast to S. cerevisiae, disruption of HpPMT1 alone caused temperature sensitivity. Inactivation of the HpPMT1 gene decreased intracellular aggregation of uPA, suggesting that enhanced secretion of uPA was due to improvement of its folding in the endoplasmic reticulum. Unlike most of the endoplasmic reticulum membrane proteins, HpPmt1p possesses the C-terminal KDEL retention signal. The GenBank Accession No. for the H. polymorpha PMT1 sequence is AY701415.

ISSN 

0749-503X

Link 

http://dx.doi.org/10.1002/yea.1297

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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