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TitleMolecular and functional characterization of an invertase secreted by Ashbya gossypii
Author(s)Aguiar, Tatiana Quinta
Dinis, Cláudia
Magalhães, Frederico
Oliveira, Carla Cristina Marques de
Wiebe, Marilyn G.
Penttilä, Merja
Domingues, Lucília
KeywordsAshbya gossypii
Glucose repression
Invertase secretion
Secretion regulation
Issue date2014
PublisherHumana Press Inc.
JournalMolecular Biotechnology
CitationAguiar, T. Q.; Dinis, C.; Magalhães, F.; Oliveira, Carla Cristina Marques de; Wiebe, M. G.; Penttilä, M.; Domingues, Lucília, Molecular and functional characterization of an invertase secreted by Ashbya gossypii. Molecular Biotechnology, 56(6), 524-534, 2014
Abstract(s)The repertoire of hydrolytic enzymes natively secreted by the filamentous fungus Ashbya (Eremothecium) gossypii has been poorly explored. Here, an invertase secreted by this flavinogenic fungus was for the first time molecularly and functionally characterized. Invertase activity was detected in A. gossypii culture supernatants and cell-associated fractions. Extracellular invertase migrated in a native polyacrylamide gel as diffuse protein bands, indicating the occurrence of at least two invertase isoforms. Hydrolytic activity towards sucrose was approximately 10 times higher than towards raffinose. Inulin and levan were not hydrolyzed. Production of invertase by A. gossypii was repressed by the presence of glucose in the culture medium. The A. gossypii invertase was demonstrated to be encoded by the AFR529W (AgSUC2) gene, which is highly homologous to the Saccharomyces cerevisiae SUC2 (ScSUC2) gene. Agsuc2 null mutants were unable to hydrolyze sucrose, proving that invertase is encoded by a single gene in A. gossypii. This mutation was functionally complemented by the ScSUC2 and AgSUC2 genes, when expressed from a 2-micron plasmid. The signal sequences of both AgSuc2p and ScSuc2p were able to direct the secretion of invertase into the culture medium in A. gossypii.
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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