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Molecular and functional characterization of an Entamoeba histolytica protein (EhMLCI) with features of a myosin essential light chain

dc.creatorMeza, Isaura
dc.creatorDíaz-Valencia, J. Daniel
dc.creatorFranco, Elizabeth
dc.creatorVillegas-Sepulveda, Nicolas
dc.creatorLezama, Ruth A.
dc.creatorBenitez-King, Gloria
dc.date.accessioned2017-06-30T04:00:07Z
dc.date.available2017-06-30T04:00:07Z
dc.date.issued2012es_ES
dc.identifier2442es_ES
dc.identifier.issn0166-6851es_ES
dc.identifier.urihttp://repositorio.inprf.gob.mx/handle/123456789/7083
dc.identifier.urihttps://doi.org/10.1016/j.molbiopara.2011.09.007es_ES
dc.language.isoenges_ES
dc.publisherElsevier Science BV, PO Box 211, 1000 AE Amsterdam, Netherlandses_ES
dc.relation181 (1) 17-28 p.es_ES
dc.relationversión del editores_ES
dc.rightsacceso cerradoes_ES
dc.titleMolecular and functional characterization of an Entamoeba histolytica protein (EhMLCI) with features of a myosin essential light chaines_ES
dc.typearticlees_ES
dc.contributor.affiliationIPN, Ctr Invest & Estudios Avanzados, Dept Biomed Mol, Apartado 14-740, Mexico City 07360, DF, Mexico.es_ES
dc.contributor.emailimeza@cinvestav.mxes_ES
dc.relation.jnabreviadoMOL BIOCHEM PARASITOLes_ES
dc.relation.journalMolecular and biochemical parasitologyes_ES
dc.identifier.placeAmsterdames_ES
dc.date.published2012es_ES
dc.identifier.organizacionInstituto Nacional de Psiquiatría Ramón de la Fuente Muñiz, México.es_ES
dc.identifier.eissn1872-9428es_ES
dc.identifier.doi10.1016/j.molbiopara.2011.09.007es_ES
dc.description.monthEnees_ES
dc.description.abstractotrodiomaEntamoeba histolytica, a protozoan parasite of humans, relays on its striking motility to survive and invade host tissues. Characterization of the molecular components involved in motile processes is crucial to understand its pathogenicity. Although protein components of myosin II hexamers have been predicted from E. histolytica genome data, only a heavy chain of myosin, EhmhcA, has been characterized so far. We have cloned an E. histolytica cDNA sequence that best matched Dictyostelium discoideum myosin essential light chain and found that the cloned sequence is transcribed as an mRNA of 0.445 kb which could encode a protein of 16.88 kDa, within the predicted range for a myosin light chain. In silico analyses revealed that the protein sequence, named EhMLCI, shows two consensus domains for binding MHC, but lacks the N-terminal sequence for actin binding, as in A2 type myosin essential light chains. A single EF-hand calcium-binding domain was identified in the C-terminus and several high score predictability sites for serine and tyrosine phosphorylation. Antibodies to recombinant EhMLCI identified two proteins of approximately 17 and 15 kDa in trophozoite extracts, the latter phophorylated in tyrosines. Serine phosphorylation was not detected. Immunomicroscopy revealed EhMLCI cortical and cytoplasmic distribution in trophozoites and true colocalization with EhmhcA determined by PCC. Co-immunoprecipitation corroborated EhMLCI interaction with EhmhcA. EhMLCI was also localized in actomyosin-containing complexes. Differential partition of phospho-tyrosinated EhMLCI into cell fractions containing the soluble form of EhmhcA and its lack of serine phosphorylation suggest its possible participation in a novel down regulatory mechanism of myosin II activity in E. histolytica.es_ES


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