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dc.contributor.authorFirmino, Alexandre A. P.pt_BR
dc.contributor.authorUlhoa, Cirano Josépt_BR
dc.contributor.authorSousa, Marcelo Valle dept_BR
dc.contributor.authorFerreira Filho, Edivaldo Ximenespt_BR
dc.contributor.authorRicart, Carlos André Ornelaspt_BR
dc.date.accessioned2017-12-07T04:37:05Z-
dc.date.available2017-12-07T04:37:05Z-
dc.date.issued2002pt_BR
dc.identifier.citationFIRMINO, Alexandre A. P. et al. Involvement of G proteins and cAMP in the production of chitinolytic enzymes by Trichoderma harzianum. Brazilian Journal of Microbiology, v. 33, n. 2, p. 169-173, 2002. DOI: https://doi.org/10.1590/S1517-83822002000200015. Disponível em: https://www.scielo.br/j/bjm/a/zXzdCBVfcP5XSKPLM6PT9rv/?lang=en#. Acesso em: 10 set. 2021.pt_BR
dc.identifier.urihttp://repositorio.unb.br/handle/10482/25950-
dc.language.isoenpt_BR
dc.publisherSociedade Brasileira de Microbiologiapt_BR
dc.rightsAcesso Abertopt_BR
dc.titleInvolvement of G proteins and cAMP in the production of chitinolytic enzymes by Trichoderma harzianumpt_BR
dc.title.alternativeEnvolvimento de proteínas G e cAMP na produção de enzimas quitinolíticas por Trichoderma harzianum-
dc.typeArtigopt_BR
dc.subject.keywordTrichoderma harzianumpt_BR
dc.subject.keywordEnzimaspt_BR
dc.subject.keywordProteínaspt_BR
dc.rights.licenseBrazilian Journal of Microbiology - This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY NC). Fonte: https://www.scielo.br/j/bjm/a/zXzdCBVfcP5XSKPLM6PT9rv/?lang=en#. Acesso em: 10 set. 2021.-
dc.identifier.doihttps://dx.doi.org/10.1590/S1517-83822002000200015pt_BR
dc.description.abstract1The effect of G protein modulators and cyclic AMP (cAMP) on N-acetylglucosaminidase (NAGase) production was investigated during 84 h of growth of a Trichoderma harzianum strain in chitin-containing medium. Caffeine (5 mM), N6--2'-O-dibutyryladenosine 3'5'-cyclic monophosphate sodium salt (dBcAMP) (1 mM) and 3-isobutyl-1-methylxanthine (IBMX) (2 mM) decreased extracellular NAGase activity by 80%, 77% and 37%, respectively. AlCl3/KF (100 µM/10 mM and 200 µM/ 20 mM) decreased the activity by 85% and 95%, respectively. Cholera (10 µ/mL) and pertussis (20 µ/mL) toxins also affected NAGase activity, causing a decrease of approximately 75%. Upon all treatments, protein bands of approximately 73 kDa, 68 kDa and 45 kDa had their signals diminished whilst a 50 kDa band was enhanced only by treatment with cholera and pertussis toxins. N-terminal sequencing analysis identified the 73 kDa and 68 kDa proteins as being T. harzianum NAGase in two different truncated forms whereas the 45 kDa band comprised a T. harzianum endochitinase. The 50 kDa protein showed sequence similarity to Coriolus vesicolor cellobiohydrolase. The above results suggest that a signaling pathway comprising G-proteins, adenylate cyclase and cAMP may be involved in the synthesis of T. harzianum chitinases.-
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