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Broad-spectrum ubiquitin/ubiquitin-like deconjugation activity of the rhizobial effector NopD from Bradyrhizobium (sp. XS1150).
Li, Ying; Perez-Gil, Jordi; Lois, L Maria; Varejão, Nathalia; Reverter, David.
Afiliação
  • Li Y; Institut de Biotecnologia i de Biomedicina and Dept. de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
  • Perez-Gil J; Qingdao University, 266071, Qingdao, China.
  • Lois LM; Center for Research in Agricultural Genomics-CRAG, Edifici CRAG-Campus UAB, 08193, Bellaterra, Barcelona, Spain.
  • Varejão N; ARC Centre of Excellence in Synthetic Biology and Centre for Agriculture and the Bioeconomy, Queensland University of Technology, Brisbane, QLD, 4000, Australia.
  • Reverter D; Center for Research in Agricultural Genomics-CRAG, Edifici CRAG-Campus UAB, 08193, Bellaterra, Barcelona, Spain.
Commun Biol ; 7(1): 644, 2024 May 27.
Article em En | MEDLINE | ID: mdl-38802699
ABSTRACT
The post-translational modification of proteins by ubiquitin-like modifiers (UbLs), such as SUMO, ubiquitin, and Nedd8, regulates a vast array of cellular processes. Dedicated UbL deconjugating proteases families reverse these modifications. During bacterial infection, effector proteins, including deconjugating proteases, are released to disrupt host cell defenses and promote bacterial survival. NopD, an effector protein from rhizobia involved in legume nodule symbiosis, exhibits deSUMOylation activity and, unexpectedly, also deubiquitination and deNeddylation activities. Here, we present two crystal structures of Bradyrhizobium (sp. XS1150) NopD complexed with either Arabidopsis SUMO2 or ubiquitin at 1.50 Å and 1.94 Å resolution, respectively. Despite their low sequence similarity, SUMO and ubiquitin bind to a similar NopD interface, employing a unique loop insertion in the NopD sequence. In vitro binding and activity assays reveal specific residues that distinguish between deubiquitination and deSUMOylation. These unique multifaceted deconjugating activities against SUMO, ubiquitin, and Nedd8 exemplify an optimized bacterial protease that disrupts distinct UbL post-translational modifications during host cell infection.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Bradyrhizobium / Ubiquitina Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Bradyrhizobium / Ubiquitina Idioma: En Ano de publicação: 2024 Tipo de documento: Article