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

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

Author Marem, Alyne Autor UNIFESP Google Scholar
Okamoto, Débora Noma Autor UNIFESP Google Scholar
Oliveira, Lilian Caroline Gonçalves de Autor UNIFESP Google Scholar
Ruiz, Diego M. Google Scholar
Paggi, Roberto A. Google Scholar
Kondo, Marcia Yuri Autor UNIFESP Google Scholar
Gouvea, Iuri Estrada Autor UNIFESP Google Scholar
Juliano, Maria Aparecida Autor UNIFESP Google Scholar
Castro, Rosana E. de Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Icimoto, Marcelo Yudi Autor UNIFESP Google Scholar
Abstract Nep (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.
Keywords Serine protease
Natrialba magadii
Haloalkaliphilic protease
Language English
Sponsor Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
Argentinian research agency Ministerio de Ciencia, Tecnologia e Innovacion Productiva (MINCyT) (Cooperative Research Project MINCyT-CAPES)
Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET), Argentina
Grant number FAPESP: 2015/01829-4
CNPq: 33009015001P0
MINCyT-CAPES: BR09/04
CONICET: PIP-1783
Date 2018
Published in International Journal Of Biological Macromolecules. Amsterdam, v. 113, p. 1134-1141, 2018.
ISSN 0141-8130 (Sherpa/Romeo, impact factor)
Publisher Elsevier Science Bv
Extent 1134-1141
Origin http://dx.doi.org/10.1016/j.ijbiomac.2018.03.026
Access rights Closed access
Type Article
Web of Science ID WOS:000432503100129
URI http://repositorio.unifesp.br/handle/11600/45967

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