Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.

Detalhes bibliográficos
Autor(a) principal: Sá-Nogueira, Isabel de
Data de Publicação: 2008
Outros Autores: Inácio, José Manuel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/4201
Resumo: Journal of Bacteriology (Junho 2008) 4272-4280
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spelling Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.Journal of Bacteriology (Junho 2008) 4272-4280The extracellular depolymerization of arabinopolysaccharides by microorganisms is accomplished by arabinanases, xylanases, and galactanases. Here, we characterize a novel endo-alpha-1,5-l-arabinanase (EC 3.2.1.99) from Bacillus subtilis, encoded by the yxiA gene (herein renamed abn2) that contributes to arabinan degradation. Functional studies by mutational analysis showed that Abn2, together with previously characterized AbnA, is responsible for the majority of the extracellular arabinan activity in B. subtilis. Abn2 was overproduced in Escherichia coli, purified from the periplasmic fraction, and characterized with respect to substrate specificity and biochemical and physical properties. With linear-alpha-1,5-l-arabinan as the preferred substrate, the enzyme exhibited an apparent K(m) of 2.0 mg ml(-1) and V(max) of 0.25 mmol min(-1) mg(-1) at pH 7.0 and 50 degrees C. RNA studies revealed the monocistronic nature of abn2. Two potential transcriptional start sites were identified by primer extension analysis, and both a sigma(A)-dependent and a sigma(H)-dependent promoter were located. Transcriptional fusion studies revealed that the expression of abn2 is stimulated by arabinan and pectin and repressed by glucose; however, arabinose is not the natural inducer. Additionally, trans-acting factors and cis elements involved in transcription were investigated. Abn2 displayed a control mechanism at a level of gene expression different from that observed with AbnA. These distinct regulatory mechanisms exhibited by two members of extracellular glycoside hydrolase family 43 (GH43) suggest an adaptative strategy of B. subtilis for optimal degradation of arabinopolysaccharides.This work was partially supported by grant no. POCI/AGR/60236/2004 from Fundacao para a Ciencia e Tecnologia (FCT) and FEDER to I.D.S.-N. and by fellowship SFRH/BD/18238/2004 from FCT to J.M.I.American Society for MicrobiologyRUNSá-Nogueira, Isabel deInácio, José Manuel2010-10-25T11:03:53Z2008-042008-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/4201engInácio, J.M., and I. de Sá-Nogueira. (2008). Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation. Journal of Bacteriology 190: 4272-4280.0021-9193 (Print)info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T03:33:53Zoai:run.unl.pt:10362/4201Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:15:35.635749Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
title Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
spellingShingle Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
Sá-Nogueira, Isabel de
title_short Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
title_full Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
title_fullStr Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
title_full_unstemmed Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
title_sort Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation.
author Sá-Nogueira, Isabel de
author_facet Sá-Nogueira, Isabel de
Inácio, José Manuel
author_role author
author2 Inácio, José Manuel
author2_role author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Sá-Nogueira, Isabel de
Inácio, José Manuel
description Journal of Bacteriology (Junho 2008) 4272-4280
publishDate 2008
dc.date.none.fl_str_mv 2008-04
2008-04-01T00:00:00Z
2010-10-25T11:03:53Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/4201
url http://hdl.handle.net/10362/4201
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Inácio, J.M., and I. de Sá-Nogueira. (2008). Characterization of the abn2(yxiA) encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharides degradation. Journal of Bacteriology 190: 4272-4280.
0021-9193 (Print)
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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