Molecular and functional characterization of an Entamoeba histolytica protein (EhMLCI) with features of a myosin essential light chain
Por:
Meza I., Díaz-Valencia J.D., Franco E., Villegas-Sepúlveda N., Lezama R.A., Benítez-King G.
Publicada:
1 ene 2012
Resumen:
Entamoeba 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 hi
Filiaciones:
Meza I.:
IPN, Ctr Invest & Estudios Avanzados, Dept Biomed Mol, Mexico City 07360, DF, Mexico
Díaz-Valencia J.D.:
IPN, Ctr Invest & Estudios Avanzados, Dept Biomed Mol, Mexico City 07360, DF, Mexico
Franco E.:
IPN, Ctr Invest & Estudios Avanzados, Dept Biomed Mol, Mexico City 07360, DF, Mexico
Villegas-Sepúlveda N.:
IPN, Ctr Invest & Estudios Avanzados, Dept Biomed Mol, Mexico City 07360, DF, Mexico
Lezama R.A.:
Escuela Nacional de Ciencias Biológicas, IPN, México DF, Mexico
Benítez-King G.:
Instituto Nacional de Psiquiatría, Departamento de Neurofarmacología, Subdirección de Investigaciones Clínicas, México DF, Mexico
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