Functional roles of C-terminal extension (CTE) of salt-dependent peptidase activity of the Natrialba magadii extracellular protease (NEP)

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dc.contributor.authorMarem, Alyne [UNIFESP]
dc.contributor.authorOkamoto, Débora Noma [UNIFESP]
dc.contributor.authorOliveira, Lilian Caroline Gonçalves de [UNIFESP]
dc.contributor.authorRuiz, Diego M.
dc.contributor.authorPaggi, Roberto A.
dc.contributor.authorKondo, Marcia Yuri [UNIFESP]
dc.contributor.authorGouvea, Iuri Estrada [UNIFESP]
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorCastro, Rosana E. de
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorIcimoto, Marcelo Yudi [UNIFESP]
dc.date.accessioned2018-07-26T12:18:26Z
dc.date.available2018-07-26T12:18:26Z
dc.date.issued2018
dc.description.abstractNep (Natrialba magadii extracellular protease) is a halolysin-like peptidase secreted by the haloalkaliphilic archaeon Natrialba magadii. Many extracellular proteases have been characterized from archaea to bacteria as adapted to hypersaline environments retaining function and stability until 4.0 M NaCI. As observed in other secreted halolysins, this stability can be related to the presence of a C-terminal extension (CTE) sequence. In the present work, we compared the biochemical properties of recombinant Nep protease with the truncated form at the 134 amino acids CTE (Nep Delta KTE), that was more active in 4 M NaCI than the non-truncated wild type enzyme. Comparable to the wild type, Nep Delta CTE protease is irreversibly inactivated at low salt solutions. The substrate specificity of the truncated Nep Delta CTE was similar to that of wild type form as demonstrated by a combinatorial library of FRET substrates. The enzyme stability, the effect of different salts and the thermodynamics assays using different lengths of substrates demonstrated similarities between the two forms. Altogether, these data provide further information on the stability and structural determinants of halolysins under different salinities, especially concerning the enzymatic behavior. (C) 2018 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Fed Sao Paulo, Escola Paulista Med, Dept Biofis, Rua Tres Maio 100, BR-04044020 Sao Paulo, Brazil
dc.description.affiliationUniv Nacl San Martin, Inst Invest Biotecnol Chascomus, Chascomus, Argentina
dc.description.affiliationUniv Nacl Mar Plata, IIB, Mar Del Plata, Argentina
dc.description.affiliationUnifespUniv Fed Sao Paulo, Escola Paulista Med, Dept Biofis, Rua Tres Maio 100, BR-04044020 Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
dc.description.sponsorshipCoordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
dc.description.sponsorshipArgentinian research agency Ministerio de Ciencia, Tecnologia e Innovacion Productiva (MINCyT) (Cooperative Research Project MINCyT-CAPES)
dc.description.sponsorshipConsejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET), Argentina
dc.description.sponsorshipIDFAPESP: 2015/01829-4
dc.description.sponsorshipIDCNPq: 33009015001P0
dc.description.sponsorshipIDMINCyT-CAPES: BR09/04
dc.description.sponsorshipIDCONICET: PIP-1783
dc.format.extent1134-1141
dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2018.03.026
dc.identifier.citationInternational Journal Of Biological Macromolecules. Amsterdam, v. 113, p. 1134-1141, 2018.
dc.identifier.doi10.1016/j.ijbiomac.2018.03.026
dc.identifier.issn0141-8130
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/45967
dc.identifier.wosWOS:000432503100129
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectSerine proteaseen
dc.subjectNatrialba magadiien
dc.subjectHaloalkaliphilic proteaseen
dc.titleFunctional roles of C-terminal extension (CTE) of salt-dependent peptidase activity of the Natrialba magadii extracellular protease (NEP)en
dc.typeinfo:eu-repo/semantics/article
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