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Updated: Aug 10, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
[Comparative structural analysis of myosin light chains and gene duplication in fish]
Abstract:
Origin and structure of myosin light chain (MLC) proteins have been studied by comparative analysis of fish mlc1, mlc2, and mlc3 genes encoding MLC1, MLC2, and MLC3, respectively. The exon-intron structure of these genes has been analyzed in zebrafish Danio rerio, loach Misgurnus fossilis, fugu Takifugu rubripes, and Nile puffer Tetraodon fahaka. We propose that mlc1 and mlc3 are homologues genes originated by fish-specific whole genome duplication (paralogs). This is supported by high sequence similarity between mlc1 and mlc3 as well as by the exon-intron structure of these genes and their localization on different chromosomes. Exons 2 to 5 of mlc1 and mlc3 are highly conserved and have similar splicing sites. A paralog gene of mlc2 resulting from a similar duplication event has been identified in zebrafish genome. Expression of mlc2 paralog is limited to the larval stages of Danio rerio and to regenerating tissues of the adult fish. There is a possibility that the paralog of mlc2 encodes larval myosin light chain protein (larval MLC) previously reported in a number of fish species.
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