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

Background: 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...

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Autores:
Ospina Garcia, Katterine
Corredor Rozo, Zayda Lorena
Marquez-Ortiz, Ricaurte Alejandro
Castellanos, Jaime
Vanegas, Natasha
Escobar-Pérez, Javier
Tipo de recurso:
Fecha de publicación:
2019
Institución:
Universidad El Bosque
Repositorio:
Repositorio U. El Bosque
Idioma:
eng
OAI Identifier:
oai:repositorio.unbosque.edu.co:20.500.12495/1681
Acceso en línea:
http://hdl.handle.net/20.500.12495/1681
http://doi.org/10.2174/1875036201912010018
Palabra clave:
Bacillus subtilis
Estructura molecular
Infecciones estafilocócicas
Biofilm
Com_YlbF domain
YheA/Qrp protein
Rights
License
Attribution 4.0 International
id UNBOSQUE2_b3f1c39a7bce8732649cdd57ce780f1e
oai_identifier_str oai:repositorio.unbosque.edu.co:20.500.12495/1681
network_acronym_str UNBOSQUE2
network_name_str Repositorio U. El Bosque
repository_id_str
dc.title.spa.fl_str_mv Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
title Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
spellingShingle Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
Bacillus subtilis
Estructura molecular
Infecciones estafilocócicas
Biofilm
Com_YlbF domain
YheA/Qrp protein
title_short Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
title_full Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
title_fullStr Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
title_full_unstemmed Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
title_sort Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureus
dc.creator.fl_str_mv Ospina Garcia, Katterine
Corredor Rozo, Zayda Lorena
Marquez-Ortiz, Ricaurte Alejandro
Castellanos, Jaime
Vanegas, Natasha
Escobar-Pérez, Javier
dc.contributor.author.none.fl_str_mv Ospina Garcia, Katterine
Corredor Rozo, Zayda Lorena
Marquez-Ortiz, Ricaurte Alejandro
Castellanos, Jaime
Vanegas, Natasha
Escobar-Pérez, Javier
dc.contributor.orcid.none.fl_str_mv Castellanos, Jaime [0000-0003-1596-8383]
Escobar-Pérez, Javier [0000-0002-0432-6978]
dc.subject.decs.spa.fl_str_mv Bacillus subtilis
Estructura molecular
Infecciones estafilocócicas
topic Bacillus subtilis
Estructura molecular
Infecciones estafilocócicas
Biofilm
Com_YlbF domain
YheA/Qrp protein
dc.subject.keywords.spa.fl_str_mv Biofilm
Com_YlbF domain
YheA/Qrp protein
description Background: 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.
publishDate 2019
dc.date.accessioned.none.fl_str_mv 2019-09-13T14:10:34Z
dc.date.available.none.fl_str_mv 2019-09-13T14:10:34Z
dc.date.issued.none.fl_str_mv 2019
dc.type.spa.fl_str_mv article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.local.spa.fl_str_mv artículo
dc.identifier.issn.none.fl_str_mv 1875-0362
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/20.500.12495/1681
dc.identifier.doi.none.fl_str_mv http://doi.org/10.2174/1875036201912010018
dc.identifier.instname.spa.fl_str_mv instname:Universidad El Bosque
dc.identifier.reponame.spa.fl_str_mv reponame:Repositorio Institucional Universidad El Bosque
dc.identifier.repourl.none.fl_str_mv repourl:https://repositorio.unbosque.edu.co
identifier_str_mv 1875-0362
instname:Universidad El Bosque
reponame:Repositorio Institucional Universidad El Bosque
repourl:https://repositorio.unbosque.edu.co
url http://hdl.handle.net/20.500.12495/1681
http://doi.org/10.2174/1875036201912010018
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.ispartofseries.spa.fl_str_mv Open Bioinformatics Journal, 1875-0362, Vol. 12, 2019, p. 18-29
dc.relation.uri.none.fl_str_mv https://openbioinformaticsjournal.com/VOLUME/12/PAGE/18/
dc.rights.*.fl_str_mv Attribution 4.0 International
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.uri.*.fl_str_mv http://creativecommons.org/licenses/by/4.0/
dc.rights.local.spa.fl_str_mv Acceso abierto
dc.rights.accessrights.none.fl_str_mv http://purl.org/coar/access_right/c_abf408
dc.rights.creativecommons.none.fl_str_mv 2019
rights_invalid_str_mv Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
Acceso abierto
http://purl.org/coar/access_right/c_abf408
2019
http://purl.org/coar/access_right/c_abf2
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Bentham science publishers
dc.publisher.journal.spa.fl_str_mv Open Bioinformatics Journal
institution Universidad El Bosque
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spelling Ospina Garcia, KatterineCorredor Rozo, Zayda LorenaMarquez-Ortiz, Ricaurte AlejandroCastellanos, JaimeVanegas, NatashaEscobar-Pérez, JavierCastellanos, Jaime [0000-0003-1596-8383]Escobar-Pérez, Javier [0000-0002-0432-6978]2019-09-13T14:10:34Z2019-09-13T14:10:34Z20191875-0362http://hdl.handle.net/20.500.12495/1681http://doi.org/10.2174/1875036201912010018instname:Universidad El Bosquereponame:Repositorio Institucional Universidad El Bosquerepourl:https://repositorio.unbosque.edu.coapplication/pdfengBentham science publishersOpen Bioinformatics JournalOpen Bioinformatics Journal, 1875-0362, Vol. 12, 2019, p. 18-29https://openbioinformaticsjournal.com/VOLUME/12/PAGE/18/Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/Acceso abiertohttp://purl.org/coar/access_right/c_abf4082019http://purl.org/coar/access_right/c_abf2Identification and “in silico” structural analysis of the glutamine-rich protein Qrp (YheA) in staphylococcus aureusarticleartículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Bacillus subtilisEstructura molecularInfecciones estafilocócicasBiofilmCom_YlbF domainYheA/Qrp proteinBackground: 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.ORIGINALEscobar-Perez J., Ospina-Garcia K., Rozo Z.L.C., Marquez-Ortiz R.A., Castellanos J.E., Gomez N.V._2019.pdfEscobar-Perez J., Ospina-Garcia K., Rozo Z.L.C., Marquez-Ortiz R.A., Castellanos J.E., Gomez N.V._2019.pdfapplication/pdf6632510https://repositorio.unbosque.edu.co/bitstreams/ac094845-2524-40aa-acc4-c10ce6ebbe7f/downloadd172d4be16e9a52b3908c9520ea76a3eMD51CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8908https://repositorio.unbosque.edu.co/bitstreams/986d4bf1-cdaf-4052-8853-c8e6c67ad47f/download0175ea4a2d4caec4bbcc37e300941108MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://repositorio.unbosque.edu.co/bitstreams/7eaa199a-14d6-450a-94fa-fddb4efd7297/download8a4605be74aa9ea9d79846c1fba20a33MD53THUMBNAILEscobar-Perez J., Ospina-Garcia K., Rozo Z.L.C., Marquez-Ortiz R.A., Castellanos J.E., Gomez N.V._2019.pdf.jpgEscobar-Perez J., Ospina-Garcia K., Rozo Z.L.C., Marquez-Ortiz R.A., Castellanos J.E., Gomez N.V._2019.pdf.jpgIM Thumbnailimage/jpeg9251https://repositorio.unbosque.edu.co/bitstreams/aa6d886d-2cba-4b70-90c5-dceab473f83e/downloada45ade7d3959765b689bb8fa3e6c3614MD54TEXTEscobar-Perez J., Ospina-Garcia K., Rozo Z.L.C., Marquez-Ortiz R.A., Castellanos J.E., Gomez N.V._2019.pdf.txtEscobar-Perez J., Ospina-Garcia K., Rozo Z.L.C., Marquez-Ortiz R.A., Castellanos J.E., Gomez N.V._2019.pdf.txtExtracted texttext/plain56013https://repositorio.unbosque.edu.co/bitstreams/74022c42-0709-4788-a79c-593bf6da2747/download0aeab130860afcfbe268d109d023e626MD5520.500.12495/1681oai:repositorio.unbosque.edu.co:20.500.12495/16812024-02-07 02:44:39.493http://creativecommons.org/licenses/by/4.0/Attribution 4.0 Internationalopen.accesshttps://repositorio.unbosque.edu.coRepositorio Institucional Universidad El Bosquebibliotecas@biteca.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