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Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition
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SYSNO ASEP 0394743 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition Tvůrce(i) Vinterová, Zuzana (UOCHB-X)
Bauerová, Václava (UOCHB-X)
Dostál, Jiří (UOCHB-X) RID, ORCID
Sychrová, Hana (FGU-C) RID, ORCID
Hrušková-Heidingsfeldová, Olga (UOCHB-X) RID, ORCID
Pichová, Iva (UOCHB-X) RID, ORCIDCelkový počet autorů 6 Zdroj.dok. Journal of Microbiology. - : Microbiological society of Korea - ISSN 1225-8873
Roč. 51, č. 3 (2013), s. 336-344Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. KR - Korejská republika Klíč. slova Candida parapsilosis ; Saccharomyces cerevisiae ; secreted aspartic proteinase ; SAPP1 ; nitrogen metabolism Vědní obor RIV EE - Mikrobiologie, virologie Vědní obor RIV – spolupráce Fyziologický ústav - Mikrobiologie, virologie CEP GA310/09/1945 GA ČR - Grantová agentura ČR GAP302/12/1151 GA ČR - Grantová agentura ČR Institucionální podpora UOCHB-X - RVO:61388963 ; FGU-C - RVO:67985823 UT WOS 000321134100011 EID SCOPUS 84879612563 DOI 10.1007/s12275-013-2422-4 Anotace 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 sequence under 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 this plasmid secreted a low concentration of active proteinase regardless of the type of nitrogen source used. Quantitative real-time PCR analysis of a set of genes related to nitrogen metabolism and uptake (GAT1, GLN3, STP2, GAP1, OPT1, and PTR2) obtained from S. cerevisiae cells transformed with either plasmid encoding SAPP1 under control of its own promoter or empty vector and cultivated in media containing various nitrogen sources also suggested that SAPP1 expression can be connected with the S. cerevisiae regulatory network. However, this regulation occurs in a different manner than in C. parapsilosis. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2014
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