KAR3, a kinesin-related gene required for yeast nuclear fusion
Abstract
The KAR3 gene is essential for yeast nuclear fusion during mating, and its expression is strongly induced by alpha factor. The predicted KAR3 protein sequence contains two globular domains separated by an alpha-helical coiled coil. The carboxy-terminal domain is homologous to the amino-terminal mechanochemical domain of Drosophila kinesin heavy chain. Mutation of the putative ATP binding site produces a dominant "poison" of nuclear fusion. The mutant protein shows enhanced microtubule association in vivo, as predicted for a kinesin-like protein in a state of rigor binding. Localization of hybrid proteins to cytoplasmic microtubules in shmoos indicates that the amino-terminal domain also contains determinants for microtubule association. Thus, KAR3 is a member of a larger family of kinesin-like proteins characterized by the presence of the mechanochemical domain tethered to different protein binding domains. The phenotypes of kar3 mutants suggest that the protein mediates microtubule sliding during nuclear fusion and possibly mitosis.
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The motor domains of Pkl1 are similar in sequence to the Saccharomyces cerevisiae kinesin-14A motor Kar3.
“The motor domains of Pkl1 are similar in sequence to the Saccharomyces cerevisiae kinesin-14A motor Kar3 (16)”
From Diffusion and Directed Movement (2008) · cites this paper as [16]
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- Authors
- Meluh, P.
- Affiliations
- Princeton University (US)
- Corresponding author
- Meluh, P
- ORCID
- Meluh, P
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1990-03-23
- Volume
- 60
- Issue
- 6
- Pages
- 1029-1041
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2003771584
- Cited by
- 503
- References
- 68
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 1 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 5 · 2017: 3 · 2016: 5 · 2015: 10 · 2014: 6 · 2013: 9 · 2012: 13
- FWCI
- 23.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (GM 37739, R01GM037739)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- kinesin-like protein, nuclear fusion, mating, alpha-factor, yeast, microtubule sliding, ATP binding site, coiled coil, mitosis
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Base Sequence, Binding Sites, Cell Nucleus, Fungal Proteins, Genes, Fungal, Genetic Complementation Test, Genotype, Microtubule-Associated Proteins, Molecular Sequence Data, Mutation, Phenotype, Plasmids, Protein Conformation, RNA, Messenger, Saccharomyces cerevisiae, Sequence Homology, Nucleic Acid, Restriction Mapping, Kinesins, Saccharomyces cerevisiae Proteins
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