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Molecular modeling and in silico characterization of Mycobacterium tuberculosis TlyA : Possible misannotation of this tubercle bacilli-hemolysin

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dc.creatorArenas, Nelson E
dc.creatorSalazar, Luz M
dc.creatorSoto, Carlos Y
dc.creatorVizcaíno, Carolina
dc.creatorPatarroyo, Manuel E.
dc.creatorPatarroyo, Manuel A.
dc.creatorGómez, Arley
dc.creator.googleArenas, Nelson Espa
dc.creator.googleSalazar, Luz Mspa
dc.creator.googleSoto, Carlos Yspa
dc.creator.googleVizcaíno, Carolinaspa
dc.creator.googlePatarroyo, Manuel Espa
dc.creator.googlePatarroyo, Manuel Aspa
dc.creator.googleGámez, Arleyspa
dc.date.accessioned2020-05-07T04:31:39Z
dc.date.available2020-05-07T04:31:39Z
dc.date.created2011
dc.date.issued2011
dc.description.abstractBackground: The TlyA protein has a controversial function as a virulence factor in Mycobacterium tuberculosis (M. tuberculosis). At present, its dual activity as hemolysin and RNA methyltransferase in M. tuberculosis has been indirectly proposed based on in vitro results. There is no evidence however for TlyA relevance in the survival of tubercle bacilli inside host cells or whether both activities are functionally linked. A thorough analysis of structure prediction for this mycobacterial protein in this study shows the need for reevaluating TlyA's function in virulence. Results: Bioinformatics analysis of TlyA identified a ribosomal protein binding domain (S4 domain), located between residues 5 and 68 as well as an FtsJ-like methyltranferase domain encompassing residues 62 and 247, all of which have been previously described in translation machinery-associated proteins. Subcellular localization prediction showed that TlyA lacks a signal peptide and its hydrophobicity profile showed no evidence of transmembrane helices. These findings suggested that it may not be attached to the membrane, which is consistent with a cytoplasmic localization. Three-dimensional modeling of TlyA showed a consensus structure, having a common core formed by a six-stranded β-sheet between two α-helix layers, which is consistent with an RNA methyltransferase structure. Phylogenetic analyses showed high conservation of the tlyA gene among Mycobacterium species. Additionally, the nucleotide substitution rates suggested purifying selection during tlyA gene evolution and the absence of a common ancestor between TlyA proteins and bacterial pore-forming proteins. Conclusion: Altogether, our manual in silico curation suggested that TlyA is involved in ribosomal biogenesis and that there is a functional annotation error regarding this protein family in several microbial and plant genomes, including the M. tuberculosis genome. © 2011 Arenas et al; licensee BioMed Central Ltd.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1186/1472-6807-11-16
dc.identifier.issn1472-6807
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/21885
dc.language.isoengspa
dc.relation.citationTitleBMC Structural Biology
dc.relation.citationVolumeVol. 11
dc.relation.ispartofBMC Structural Biology, ISSN: 1472-6807 Vol. 11, (2011)spa
dc.relation.urihttps://bmcstructbiol.biomedcentral.com/articles/10.1186/1472-6807-11-16spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subjectTuberculosisspa
dc.subject.ddcEnfermedadesspa
dc.subject.keywordAdoMetspa
dc.subject.keywordMycobacterium Speciesspa
dc.subject.keywordSubcellular Localization Predictionspa
dc.titleMolecular modeling and in silico characterization of Mycobacterium tuberculosis TlyA : Possible misannotation of this tubercle bacilli-hemolysinspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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