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| Genes Cells Oct (2008); 13(10):1015-26 | |
| Identification and characterization of a Jem1p ortholog of Candida albicans- dissection of Jem1p functions in karyogamy and protein quality control in Saccharomyces cerevisiae- | |
| Makio T, Nishikawa S, Nakayama T, Nagai H, Endo T | |
| Department of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan- | |
| Abstract: Jem1p of yeast Saccharomyces cerevisiae is a J-domain containing co-chaperone -J protein- in the endoplasmic reticulum -ER- lumen- Jem1p is required for nuclear fusion during mating -karyogamy- and functions together with another J protein, Scj1p, in protein folding and quality control in the ER as a partner for the ER Hsp70 -BiP-Kar2p-- Candida albicans has a gene encoding a homolog of S- cerevisiae Jem1p, CaJem1p- CaJem1p localized in the ER when expressed in S- cerevisiae, and expression of CaJem1p from a single-copy plasmid suppressed the temperature sensitive growth and the ER quality control defect of the jem1Deltascj1Delta mutant, indicating that CaJem1p is functional in S- cerevisiae- However, CaJem1p suppressed the karyogamy defect of the jem1Deltamutant only when it was over-expressed from a multicopy plasmid- Domain-swapping experiments showed that this was due to the difference between the N-terminal domains of ScJem1p and CaJem1p- The N-terminal domain of ScJem1p is essential for its function and interacts with Nep98p, a component of the spindle pole body involved in karyogamy- Since the interaction of CaJem1p with Nep98p is weaker than that of ScJem1p, the Nep98p-ScJem1p interaction is likely important for promoting karyogamy in S- cerevisiae- | |
| [PUBMED: 18754794] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |