Abstract
Cytoplasmic dynein is a multisubunit, microtubule-dependent motor enzyme that has been proposed to function in a variety of intracellular movements. As part of an effort to understand the evolution and the biological roles of cytoplasmic dynein, we have identified the first non-metazoan dynein light chain 1, SLC1, in the yeastSaccharomyces cerevisiae. The amino acid sequence of the SLC1 protein is similar to those of the human,Drosophila andCaenorhabditis cytoplasmic dynein light chains 1. TheSLC1 gene lies adjacent to theYAP2 (CAD1) transcription unit. TheSLC1 coding sequence is split by two introns and its mRNA is detectable throughout the cell cycle. Tetrad analysis of heterozygotes harboring aTRP insertion in theSLC1 coding region indicate thatSLC1 function is not essential for cell viability. Furthermore, we demonstrate that double mutants, defective forSLC1 and the kinesin-relatedCIN8 genes are non-lethal. The redundancy ofSLC1 function in yeast contrasts with the cell death caused by loss-of-function mutations in the dynein light chain 1 gene inDrosophila melanogaster.
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Communicated by D. J. Finnegan
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Dick, T., Chia, W. & Surana, U. Molecular and genetic characterization ofSLC1, a putativeSaccharomyces cerevisiae homolog of the metazoan cytoplasmic dynein light chain 1. Molec. Gen. Genet. 251, 38–43 (1996). https://doi.org/10.1007/BF02174342
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DOI: https://doi.org/10.1007/BF02174342