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The kinesin-14 motor protein Mks1 from Caulobacter crescentus contributes to a wide range of functions including chromosome segregation and cell division. To understand the physiological function of Mks1, the effect of mutational analysis on cell growth and cytokinesis was investigated. We found that overproduction of Mks1 causes a light-independent cell elongation phenotype but the phenotype is not seen with Mks1 overexpression in a heterologous host. Mks1 overexpression affects the growth of the progeny cells in a non-cell-cycle-regulated manner. Consistent with the overproduction phenotype, overexpression of a kinase dead mutant of Mks1 results in shortened cells, suggesting that Mks1 kinase activity is required for its physiological function. Moreover, the growth defect caused by overproduction of Mks1 in the light is more severe than that in the dark, suggesting that the overproduction phenotype is light-dependent. Mutational analysis revealed the involvement of a single serine residue in phosphorylation of Mks1, Ser-16. We showed that inactivation of this serine residue abolishes cell elongation in Mks1 overproducing cells. Furthermore, the Ser-16 residue is phosphorylated in a light-dependent manner and mutation of the residue to alanine confers a dominant-negative phenotype to Mks1. Phosphorylation of Ser-16 is sufficient for the Mks1 activity, as assayed by its effect on in vitro gliding motility. Our 0b46394aab
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