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Structure and function of Campylobacter jejuni polynucleotide phosphorylase (PNPase)

2024-01Artigo científico Acesso aberto
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dc.contributor.authorBárria, Cátia
dc.contributor.authorAthayde, Diogo
dc.contributor.authorHernandez, Guillem
dc.contributor.authorFonseca, Leonor
dc.contributor.authorCasinhas, Jorge
dc.contributor.authorCordeiro, Tiago N.
dc.contributor.authorArcher, Margarida
dc.contributor.authorArraiano, Cecília M.
dc.contributor.authorBrito, José A.
dc.contributor.authorMatos, Rute G.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblElsevier Science B.V., Amsterdam.
dc.date.accessioned2025-05-08T21:31:04Z
dc.date.available2025-05-08T21:31:04Z
dc.date.issued2024-01
dc.descriptionFunding Information: This work was funded by FCT - Fundação para a Ciência e a Tecnologia, I. P., through projects MOSTMICRO-ITQB (UIDB/04612/2020 and UIDP/04612/2020), LS4FUTURE Associated Laboratory-LA/P/0087/2020, and project PTDC/BIA-BQM/28479/2017 to RGM. CB was financed by a contract under the project PTDC/BIA-BQM/28479/2017. DA and GH have a PhD fellowship from FCT with the references PD/BD/147987/2019 and PD/BD/147227/2019 (PT-NMR FCT PhD Program), respectively. JAB was financed by an FCT contract in the framework of Article 23 of Decree-Law No.57/2017 of August 29. TNC and RGM were supported by FCT contracts (CEECIND/01443/2017 and CEECIND/02065/2017, respectively). Funding Information: This work was funded by FCT - Fundação para a Ciência e a Tecnologia , I. P., through projects MOSTMICRO-ITQB ( UIDB/04612/2020 and UIDP/04612/2020 ), LS4FUTURE Associated Laboratory - LA/P/0087/2020 , and project PTDC/BIA-BQM/28479/2017 to RGM. CB was financed by a contract under the project PTDC/BIA-BQM/28479/2017. DA and GH have a PhD fellowship from FCT with the references PD/BD/147987/2019 and PD/BD/147227/2019 (PT-NMR FCT PhD Program), respectively. JAB was financed by an FCT contract in the framework of Article 23 of Decree-Law No.57/2017 of August 29. TNC and RGM were supported by FCT contracts ( CEECIND/01443/2017 and CEECIND/02065/2017 , respectively). Publisher Copyright: © 2023 The Authors
dc.description.abstractRibonucleases are in charge of the processing, degradation and quality control of all cellular transcripts, which makes them crucial factors in RNA regulation. This post-transcriptional regulation allows bacteria to promptly react to different stress conditions and growth phase transitions, and also to produce the required virulence factors in pathogenic bacteria. Campylobacter jejuni is the main responsible for human gastroenteritis in the world. In this foodborne pathogen, exoribonuclease PNPase (CjPNP) is essential for low-temperature cell survival, affects the synthesis of proteins involved in virulence and has an important role in swimming, cell adhesion/invasion ability, and chick colonization. Here we report the crystallographic structure of CjPNP, complemented with SAXS, which confirms the characteristic doughnut-shaped trimeric arrangement and evaluates domain arrangement and flexibility. Mutations in highly conserved residues were constructed to access their role in RNA degradation and polymerization. Surprisingly, we found two mutations that altered CjPNP into a protein that is only capable of degrading RNA even in conditions that favour polymerization. These findings will be important to develop new strategies to combat C. jejuni infections.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent15
dc.format.extent4709529
dc.identifier.doi10.1016/j.biochi.2023.10.006
dc.identifier.issn0300-9084
dc.identifier.otherPURE: 90690917
dc.identifier.otherPURE UUID: 49742a80-949d-4c9b-bb4e-38c249b9b326
dc.identifier.otherScopus: 85173832631
dc.identifier.otherPubMed: 37806617
dc.identifier.urihttp://hdl.handle.net/10362/182883
dc.identifier.urlhttps://www.scopus.com/pages/publications/85173832631
dc.language.isoeng
dc.peerreviewedyes
dc.subjectFoodborne pathogen
dc.subjectRibonucleases
dc.subjectRNA metabolism
dc.subjectSmall-angle X-ray scattering (SAXS)
dc.subjectX-ray crystallography
dc.subjectBiochemistry
dc.titleStructure and function of Campylobacter jejuni polynucleotide phosphorylase (PNPase)en
dc.title.subtitleInsights into the role of this RNase in pathogenicityen
dc.typejournal article
degois.publication.firstPage56
degois.publication.lastPage70
degois.publication.titleBiochimie
degois.publication.volume216
dspace.entity.typePublication
rcaap.rightsopenAccess

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