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Background : All eukaryotes with the exception of plants use an
actomyosin ring to generate a constriction force at the site of cell division
(cleavage furrow) during mitosis and meiosis. The structure and filament forming
abilities located in the C-terminal or tail region of one of the main components,
myosin II, are important for localising ... read morethe molecule to the contractile ring (CR)
during cytokinesis. However, it remains poorly understood how myosin II is recruited
to the site of cell division and how this recruitment relates to myosin filament
assembly. Significant conservation between species of the components involved in
cytokinesis, including those of the CR, allows the use of easily genetically
manipulated organisms, such as budding yeast (Saccharomyces cerevisiae), in the study
of cytokinesis. Budding yeast has a single myosin II protein, named Myo1. Unlike most
other class II myosins, the tail of Myo1 has an irregular coiled coil. In this report
we use molecular genetics, biochemistry and live cell imaging to characterize the
minimum localisation domain (MLD) of budding yeast Myo1.
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