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

Cited 15 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorM O Agaphonov-
dc.contributor.authorS S Sokolov-
dc.contributor.authorN V Romanova-
dc.contributor.authorJung Hoon Sohn-
dc.contributor.authorSo Young Kim-
dc.contributor.authorT S Kalebina-
dc.contributor.authorEui Sung Choi-
dc.contributor.authorM D Ter-Avanesyan-
dc.date.accessioned2017-04-19T09:03:43Z-
dc.date.available2017-04-19T09:03:43Z-
dc.date.issued2005-
dc.identifier.issn0749-503X-
dc.identifier.uri10.1002/yea.1297ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7206-
dc.description.abstractHuman 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.-
dc.publisherWiley-
dc.titleMutation of the protein-O-mannosyltransferase enhances secretion of the human urokinase-type plasminogen activator in Hansenula polymorpha-
dc.title.alternativeMutation of the protein-O-mannosyltransferase enhances secretion of the human urokinase-type plasminogen activator in Hansenula polymorpha-
dc.typeArticle-
dc.citation.titleYeast-
dc.citation.number13-
dc.citation.endPage1047-
dc.citation.startPage1037-
dc.citation.volume22-
dc.contributor.affiliatedAuthorJung Hoon Sohn-
dc.contributor.affiliatedAuthorSo Young Kim-
dc.contributor.affiliatedAuthorEui Sung Choi-
dc.contributor.alternativeNameAgaphonov-
dc.contributor.alternativeNameSokolov-
dc.contributor.alternativeNameRomanova-
dc.contributor.alternativeName손정훈-
dc.contributor.alternativeName김소영-
dc.contributor.alternativeNameKalebina-
dc.contributor.alternativeName최의성-
dc.contributor.alternativeNameTer-Avanesyan-
dc.identifier.bibliographicCitationYeast, vol. 22, no. 13, pp. 1037-1047-
dc.identifier.doi10.1002/yea.1297-
dc.subject.keywordEndoplasmic reticulum-
dc.subject.keywordHansenula polymorpha-
dc.subject.keywordO-mannosylation-
dc.subject.keywordProtein folding-
dc.subject.keywordProtein glycosylation-
dc.subject.keywordProtein secretion-
dc.subject.localEndoplasmic reticulum (ER)-
dc.subject.localendoplasmic reticulum (ER)-
dc.subject.localEndoplasmic reticulum-
dc.subject.localendoplasmic reticulum-
dc.subject.localHansenulapolymorpha-
dc.subject.localhansenula polymorpha-
dc.subject.localHansenula polymorpha-
dc.subject.localHansenula polymorpha (Pichia angusta)-
dc.subject.localO-mannosylation-
dc.subject.localProtein folding-
dc.subject.localprotein folding-
dc.subject.localprotein glycosylation-
dc.subject.localProtein glycosylation-
dc.subject.localProtein secretion-
dc.subject.localprotein secretion-
dc.description.journalClassY-
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.