Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus

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dc.contributor.authorOspina Garcia, Katterine
dc.contributor.authorCorredor Rozo, Zayda Lorena
dc.contributor.authorMarquez-Ortiz, Ricaurte Alejandro
dc.contributor.authorCastellanos, Jaime
dc.contributor.authorVanegas, Natasha
dc.contributor.authorEscobar-Pérez, Javier
dc.contributor.orcidCastellanos, Jaime [0000-0003-1596-8383]
dc.contributor.orcidEscobar-Pérez, Javier [0000-0002-0432-6978]
dc.date.accessioned2019-09-13T14:10:34Z
dc.date.available2019-09-13T14:10:34Z
dc.date.issued2019
dc.description.abstractenglishBackground: YlbF and YmcA are two essential proteins for the formation of biofilm, sporulation, and competence in Bacillus subtilis. In these two proteins, a new protein domain called com_ylbF was recently discovered, but its role and protein function has not yet been established. Objective: In this study, we identified and performed an “in silico” structural analysis of the YheA protein, another com_ylbF-containing protein, in the opportunistic pathogen Staphylococcus aureus. Methods: The search of the yheA gene was performed using BLAST-P and tBLASn algorithms. The three-dimensional (3D) models of YheA, as well as YlbF and YmcA proteins, were built using the I-TASSER and Quark programs. The identification of the native YheA in Staphylococcus aureus was carried out through chromatography using the FPLC system. Results: We found that YheA protein is more widely distributed in Gram-positive bacteria than YlbF and YmcA. Two new and important characteristics for YheA and other com_ylbF-containing proteins were found: a highly conserved 3D structure and the presence of a putative conserved motif located in the central region of the domain, which could be involved in its function. Additionally, we established that Staphylococcus aureus expresses YheA protein in both planktonic growth and biofilm. Finally, we suggest renaming YheA as glutamine-rich protein (Qrp) in S. aureus. Conclusion: The Grp (YheA), YlbF, and YmcA proteins adopt a highly conserved three-dimensional structure, harboring a protein-specific putative motif within the com_ylbF domain, which possibly favors the interaction with their substrates. Finally, Staphylococcus aureus expresses the Grp (YheA) protein in both planktonic and biofilm growth.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.2174/1875036201912010018
dc.identifier.instnameinstname:Universidad El Bosquespa
dc.identifier.issn1875-0362
dc.identifier.reponamereponame:Repositorio Institucional Universidad El Bosquespa
dc.identifier.repourlrepourl:https://repositorio.unbosque.edu.co
dc.identifier.urihttps://hdl.handle.net/20.500.12495/1681
dc.language.isoeng
dc.publisherBentham science publishersspa
dc.publisher.journalOpen Bioinformatics Journalspa
dc.relation.ispartofseriesOpen Bioinformatics Journal, 1875-0362, Vol. 12, 2019, p. 18-29spa
dc.relation.urihttps://openbioinformaticsjournal.com/VOLUME/12/PAGE/18/
dc.rightsAttribution 4.0 International*
dc.rights.accessrightsinfo:eu-repo/semantics/openAccess
dc.rights.accessrightshttps://purl.org/coar/access_right/c_abf408
dc.rights.creativecommons2019
dc.rights.localAcceso abiertospa
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.decsBacillus subtilisspa
dc.subject.decsEstructura molecularspa
dc.subject.decsInfecciones estafilocócicasspa
dc.subject.keywordsBiofilmspa
dc.subject.keywordsCom_YlbF domainspa
dc.subject.keywordsYheA/Qrp proteinspa
dc.titleIdentification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureusspa
dc.typearticlespa
dc.type.hasversioninfo:eu-repo/semantics/publishedVersion
dc.type.localartículospa

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Escobar-Perez J., Ospina-Garcia K., Rozo Z.L.C., Marquez-Ortiz R.A., Castellanos J.E., Gomez N.V._2019.pdf
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