Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00394743" target="_blank" >RIV/61388963:_____/13:00394743 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985823:_____/13:00394743

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s12275-013-2422-4" target="_blank" >http://dx.doi.org/10.1007/s12275-013-2422-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s12275-013-2422-4" target="_blank" >10.1007/s12275-013-2422-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition

Popis výsledku v původním jazyce

Secreted aspartic proteinase Sapp1p of Candida parapsilosis represents one of the factors contributing to the pathogenicity of the fungus. The proteinase is synthesized as an inactive pre-pro-enzyme, but only processed Sapp1p is secreted into extracellular space. We constructed a plasmid containing the SAPP1 coding sequence under control of the ScGAL1 promoter and used it for proteinase expression in a Saccharomyces cerevisiae kex2 Delta mutant. Because Sapp1p maturation depends on cleavage by Kex2p proteinase, the kex2 Delta mutant secreted only the pro-form of Sapp1p. Characterization of this secreted proteinase form revealed that the Sapp1p signal peptide consists of 23 amino acids. Additionally, we prepared a plasmid with the SAPP1 coding sequenceunder control of its authentic CpSAPP1 promoter, which contains two GATAA motifs. While in C. parapsilosis SAPP1 expression is repressed by good low molecular weight nitrogen sources (e.g., ammonium ions), S. cerevisiae cells harboring th

Název v anglickém jazyce

Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition

Popis výsledku anglicky

Secreted aspartic proteinase Sapp1p of Candida parapsilosis represents one of the factors contributing to the pathogenicity of the fungus. The proteinase is synthesized as an inactive pre-pro-enzyme, but only processed Sapp1p is secreted into extracellular space. We constructed a plasmid containing the SAPP1 coding sequence under control of the ScGAL1 promoter and used it for proteinase expression in a Saccharomyces cerevisiae kex2 Delta mutant. Because Sapp1p maturation depends on cleavage by Kex2p proteinase, the kex2 Delta mutant secreted only the pro-form of Sapp1p. Characterization of this secreted proteinase form revealed that the Sapp1p signal peptide consists of 23 amino acids. Additionally, we prepared a plasmid with the SAPP1 coding sequenceunder control of its authentic CpSAPP1 promoter, which contains two GATAA motifs. While in C. parapsilosis SAPP1 expression is repressed by good low molecular weight nitrogen sources (e.g., ammonium ions), S. cerevisiae cells harboring th

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Microbiology

ISSN

1225-8873

e-ISSN

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Svazek periodika

51

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

KR - Korejská republika

Počet stran výsledku

9

Strana od-do

336-344

Kód UT WoS článku

000321134100011

EID výsledku v databázi Scopus

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