Proceedings of the National Academy of Sciences · 1994 · 127 citations · 22 references
Life SciencesGeneticsMolecular BiologyCytoskeletonProtein FoldingProtein-protein InteractionsChaperone-assisted FoldingCytoskeletal Associated ProteinsMacromolecular AssemblyMicrotubule-associated ProteinsMolecular ChaperonesSynthetic LethalityChaperonin FunctionChaperonin-mediated FoldingChromosome Mis-segregationDefects In Microtubule PolymerizationEukaryotic ChaperonesMicrotubule DestabilizersMicrotubule-associated Protein 1Yeast Synthetic Lethality
We have isolated cold-sensitive mutations in two genes of the yeast Saccharomyces cerevisiae, BIN2 and BIN3, that cause aberrant chromosome segregation in vivo. BIN2 and BIN3 encode essential proteins that are similar to each other and to TCP-1. TCP-1 and TCP-1-like proteins are components of the eukaryotic cytoplasmic chaperonin that facilitates folding of tubulins and actin in vitro. Mutations in BIN2 and BIN3 cause defects in microtubule and actin assembly in vivo and confer supersensitivity to the microtubule-destabilizing drug benomyl. Overexpression of TCP1, BIN2, BIN3, or ANC2, a fourth member of the TCP-1 family in yeast, does not complement mutations in the other genes, indicating that the proteins have distinct functions. However, all double-mutant combinations are inviable; this synthetic lethality suggests that the proteins act in a common process. These results indicate that Bin2p and Bin3p are components of a yeast cytoplasmic chaperonin complex that is required for assembly of microtubules and actin in vivo.
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Fred Sherman · Methods in enzymology on CD-ROM/Methods in enzymology · 2002 · 3.5K citations
A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
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Phenotypic analysis of temperature-sensitive yeast actin mutants
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