Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity
Autor(a) principal: | |
---|---|
Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.3390/antiox10071032 http://hdl.handle.net/11449/233190 |
Resumo: | Typical 2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous Cys-based peroxidases, which are stable as decamers in the reduced state, and may dissociate into dimers upon disulfide bond formation. A peroxidatic Cys (CP) takes part of a catalytic triad, together with a Thr/Ser and an Arg. Previously, we described that the presence of Ser (instead of Thr) in the active site stabilizes yeast 2-Cys Prx as decamers. Here, we compared the hyperoxidation susceptibilities of yeast 2-Cys Prx. Notably, 2-Cys Prx containing Ser (named here Ser-Prx) were more resistant to hyperoxidation than enzymes containing Thr (Thr-Prx). In silico analysis revealed that Thr-Prx are more frequent in all domains of life, while Ser-Prx are more abundant in bacteria. As yeast 2-Cys Prx, bacterial Ser-Prx are more stable as decamers than Thr-Prx. However, bacterial Ser-Prx were only slightly more resistant to hyperoxidation than Thr-Prx. Furthermore, in all cases, organic hydroperoxide inhibited more the peroxidase activities of 2-Cys Prx than hydrogen peroxide. Moreover, bacterial Ser-Prx displayed increased thermal resistance and chaperone activity, which may be related with its enhanced stability as decamers compared to Thr-Prx. Therefore, the single substitution of Thr by Ser in the catalytic triad results in profound biochemical and structural differences in 2-Cys Prx. |
id |
UNSP_2a6bc84ea2f219adcd84c71eb7268076 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/233190 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
spelling |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity2-Cys PrxCatalytic triadChaperoneHyperoxidationOligomerizationOrganic hydroperoxidesTypical 2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous Cys-based peroxidases, which are stable as decamers in the reduced state, and may dissociate into dimers upon disulfide bond formation. A peroxidatic Cys (CP) takes part of a catalytic triad, together with a Thr/Ser and an Arg. Previously, we described that the presence of Ser (instead of Thr) in the active site stabilizes yeast 2-Cys Prx as decamers. Here, we compared the hyperoxidation susceptibilities of yeast 2-Cys Prx. Notably, 2-Cys Prx containing Ser (named here Ser-Prx) were more resistant to hyperoxidation than enzymes containing Thr (Thr-Prx). In silico analysis revealed that Thr-Prx are more frequent in all domains of life, while Ser-Prx are more abundant in bacteria. As yeast 2-Cys Prx, bacterial Ser-Prx are more stable as decamers than Thr-Prx. However, bacterial Ser-Prx were only slightly more resistant to hyperoxidation than Thr-Prx. Furthermore, in all cases, organic hydroperoxide inhibited more the peroxidase activities of 2-Cys Prx than hydrogen peroxide. Moreover, bacterial Ser-Prx displayed increased thermal resistance and chaperone activity, which may be related with its enhanced stability as decamers compared to Thr-Prx. Therefore, the single substitution of Thr by Ser in the catalytic triad results in profound biochemical and structural differences in 2-Cys Prx.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Instituto de Biociências Universidade Estadual Paulista UNESPDepartamento de Genética e Biologia Evolutiva Instituto de Biociências Universidade de São PauloLaboratório de Biomarcadores de Contaminação Aquática e Imunoquímica Departamento de Bioquímica Universidade Federal de Santa CatarinaLaboratório de Ecologia Molecular Instituto de Biociências Universidade Estadual Paulista UNESPInstituto de Biociências Universidade Estadual Paulista UNESPLaboratório de Ecologia Molecular Instituto de Biociências Universidade Estadual Paulista UNESPFAPESP: 2007/50930-3FAPESP: 2011/13500-6FAPESP: 2013/07937-8FAPESP: 2017/06263-4FAPESP: 2018/12628-8FAPESP: 2019/04054-4FAPESP: 2020/02868-1Universidade Estadual Paulista (UNESP)Universidade de São Paulo (USP)Universidade Federal de Santa Catarina (UFSC)Tairum, Carlos A. [UNESP]Santos, Melina Cardoso [UNESP]Breyer, Carlos Alexandre [UNESP]de Oliveira, Ana Laura Pires [UNESP]Cabrera, Vitoria Isabela Montanhero [UNESP]Toledo-Silva, GuilhermeMori, Gustavo Maruyama [UNESP]Toyama, Marcos Hikari [UNESP]Netto, Luis Eduardo Soaresde Oliveira, Marcos Antonio [UNESP]2022-05-01T05:29:33Z2022-05-01T05:29:33Z2021-07-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.3390/antiox10071032Antioxidants, v. 10, n. 7, 2021.2076-3921http://hdl.handle.net/11449/23319010.3390/antiox100710322-s2.0-85108618045Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAntioxidantsinfo:eu-repo/semantics/openAccess2022-05-01T05:29:33Zoai:repositorio.unesp.br:11449/233190Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:32:37.518716Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity |
title |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity |
spellingShingle |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity Tairum, Carlos A. [UNESP] 2-Cys Prx Catalytic triad Chaperone Hyperoxidation Oligomerization Organic hydroperoxides |
title_short |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity |
title_full |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity |
title_fullStr |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity |
title_full_unstemmed |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity |
title_sort |
Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity |
author |
Tairum, Carlos A. [UNESP] |
author_facet |
Tairum, Carlos A. [UNESP] Santos, Melina Cardoso [UNESP] Breyer, Carlos Alexandre [UNESP] de Oliveira, Ana Laura Pires [UNESP] Cabrera, Vitoria Isabela Montanhero [UNESP] Toledo-Silva, Guilherme Mori, Gustavo Maruyama [UNESP] Toyama, Marcos Hikari [UNESP] Netto, Luis Eduardo Soares de Oliveira, Marcos Antonio [UNESP] |
author_role |
author |
author2 |
Santos, Melina Cardoso [UNESP] Breyer, Carlos Alexandre [UNESP] de Oliveira, Ana Laura Pires [UNESP] Cabrera, Vitoria Isabela Montanhero [UNESP] Toledo-Silva, Guilherme Mori, Gustavo Maruyama [UNESP] Toyama, Marcos Hikari [UNESP] Netto, Luis Eduardo Soares de Oliveira, Marcos Antonio [UNESP] |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) Universidade de São Paulo (USP) Universidade Federal de Santa Catarina (UFSC) |
dc.contributor.author.fl_str_mv |
Tairum, Carlos A. [UNESP] Santos, Melina Cardoso [UNESP] Breyer, Carlos Alexandre [UNESP] de Oliveira, Ana Laura Pires [UNESP] Cabrera, Vitoria Isabela Montanhero [UNESP] Toledo-Silva, Guilherme Mori, Gustavo Maruyama [UNESP] Toyama, Marcos Hikari [UNESP] Netto, Luis Eduardo Soares de Oliveira, Marcos Antonio [UNESP] |
dc.subject.por.fl_str_mv |
2-Cys Prx Catalytic triad Chaperone Hyperoxidation Oligomerization Organic hydroperoxides |
topic |
2-Cys Prx Catalytic triad Chaperone Hyperoxidation Oligomerization Organic hydroperoxides |
description |
Typical 2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous Cys-based peroxidases, which are stable as decamers in the reduced state, and may dissociate into dimers upon disulfide bond formation. A peroxidatic Cys (CP) takes part of a catalytic triad, together with a Thr/Ser and an Arg. Previously, we described that the presence of Ser (instead of Thr) in the active site stabilizes yeast 2-Cys Prx as decamers. Here, we compared the hyperoxidation susceptibilities of yeast 2-Cys Prx. Notably, 2-Cys Prx containing Ser (named here Ser-Prx) were more resistant to hyperoxidation than enzymes containing Thr (Thr-Prx). In silico analysis revealed that Thr-Prx are more frequent in all domains of life, while Ser-Prx are more abundant in bacteria. As yeast 2-Cys Prx, bacterial Ser-Prx are more stable as decamers than Thr-Prx. However, bacterial Ser-Prx were only slightly more resistant to hyperoxidation than Thr-Prx. Furthermore, in all cases, organic hydroperoxide inhibited more the peroxidase activities of 2-Cys Prx than hydrogen peroxide. Moreover, bacterial Ser-Prx displayed increased thermal resistance and chaperone activity, which may be related with its enhanced stability as decamers compared to Thr-Prx. Therefore, the single substitution of Thr by Ser in the catalytic triad results in profound biochemical and structural differences in 2-Cys Prx. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-07-01 2022-05-01T05:29:33Z 2022-05-01T05:29:33Z |
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://dx.doi.org/10.3390/antiox10071032 Antioxidants, v. 10, n. 7, 2021. 2076-3921 http://hdl.handle.net/11449/233190 10.3390/antiox10071032 2-s2.0-85108618045 |
url |
http://dx.doi.org/10.3390/antiox10071032 http://hdl.handle.net/11449/233190 |
identifier_str_mv |
Antioxidants, v. 10, n. 7, 2021. 2076-3921 10.3390/antiox10071032 2-s2.0-85108618045 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Antioxidants |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128239985491968 |