Other names published for SIS1: YNL007C
SIS1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Regulatory Role
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Additional Information
SIS1 - Genetic Interactions (20)
| Reference | Other Genes Addressed |
|---|---|
| Kiktev DA, et al. (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70 | |
| Mathur V, et al. (2012) Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity. Mol Cell Biol 32(1):139-53 | |
| Treusch S and Lindquist S (2012) An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol 197(3):369-79 | |
| Kirkland PA, et al. (2011) Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity. Genetics 188(3):565-77 | |
| Sahi C, et al. (2010) Cwc23, an Essential J Protein Critical for Pre-mRNA Splicing with a Dispensable J Domain. Mol Cell Biol 30(1):33-42 | |
| Weeks SA, et al. (2010) A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication. J Virol 84(1):330-9 | |
| Mandal AK, et al. (2008) Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation. Mol Cell Biol 28(13):4434-44 | |
| Lian HY, et al. (2007) Hsp40 Interacts Directly with the Native State of the Yeast Prion Protein Ure2 and Inhibits Formation of Amyloid-like Fibrils. J Biol Chem 282(16):11931-40 | |
| Sahi C and Craig EA (2007) Network of general and specialty J protein chaperones of the yeast cytosol. Proc Natl Acad Sci U S A 104(17):7163-8 | |
| Gokhale KC, et al. (2005) Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J Biol Chem 280(24):22809-18 | |
| Kryndushkin DS, et al. (2002) Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277(26):23702-8 | |
| Lee S, et al. (2002) Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding. J Biol Chem 277(24):21675-82 | |
| Meriin AB, et al. (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J Cell Biol 157(6):997-1004 | |
| Horton LE, et al. (2001) The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. J Biol Chem 276(17):14426-33 | |
| Lisse T and Schwarz E (2000) Functional specificity of the mitochondrial DnaJ protein, Mdj1p, in Saccharomyces cerevisiae. Mol Gen Genet 263(3):527-34 | |
| Ohba M (1997) Modulation of intracellular protein degradation by SSB1-SIS1 chaperon system in yeast S. cerevisiae. FEBS Lett 409(2):307-11 | |
| Belostotsky DA and Meagher RB (1996) A pollen-, ovule-, and early embryo-specific poly(A) binding protein from Arabidopsis complements essential functions in yeast. Plant Cell 8(8):1261-75 | |
| Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 | |
| Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 | |
| Luke MM, et al. (1991) Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. J Cell Biol 114(4):623-38 |



