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• W2160333727 abstract "► A myosin essential-like light chain, Eh MLCI, is expressed in E. histolytica . ► Eh MLCI associates to heavy chains of amebic myosin and to actin filaments. ► Two forms of the protein are found, the minor one is phosphorylated in tyrosines. ► The phosphorylated form partitions into Triton-soluble fractions of cell extracts. ► Eh MLCI may be acting as a negative regulator of myosin activity. 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, Eh mhcA, 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 Eh MLCI, 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 Eh MLCI identified two proteins of approximately 17 and 15 kDa in trophozoite extracts, the latter phophorylated in tyrosines. Serine phosphorylation was not detected. Immunomicroscopy revealed Eh MLCI cortical and cytoplasmic distribution in trophozoites and true colocalization with Eh mhcA determined by PCC. Co-immunoprecipitation corroborated Eh MLCI interaction with Eh mhcA. Eh MLCI was also localized in actomyosin-containing complexes. Differential partition of phospho-tyrosinated E h MLCI into cell fractions containing the soluble form of Eh mhcA and its lack of serine phosphorylation suggest its possible participation in a novel down regulatory mechanism of myosin II activity in E. histolytica ." @default.
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• W2160333727 date "2012-01-01" @default.
• W2160333727 modified "2023-10-18" @default.
• W2160333727 title "Molecular and functional characterization of an Entamoeba histolytica protein (EhMLCI) with features of a myosin essential light chain" @default.
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• W2160333727 doi "https://doi.org/10.1016/j.molbiopara.2011.09.007" @default.
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