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...
- 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
- Palabra clave:
- Bacillus subtilis
Estructura molecular
Infecciones estafilocócicas
Biofilm
Com_YlbF domain
YheA/Qrp protein
- Rights
- License
- Attribution 4.0 International
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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 |
bitstream.url.fl_str_mv |
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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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 |