Difference between revisions of "YDL229W"
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+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
+ | J Biol Chem 278(5):3265-74</ref> | ||
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Revision as of 13:02, 21 February 2007
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Systematic name | YDL229W |
Gene name | SSB1 |
Aliases | YG101 |
Feature type | ORF, Verified |
Coordinates | Chr IV:44066..45907 |
Description of YDL229W: Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p[1][2][3][4][5][6][7]
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References
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- ↑ Huang P, et al. (2005) The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol 12(6):497-504 SGD PMID 15908962
- ↑ Kim SY and Craig EA (2005) Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides. Eukaryot Cell 4(1):82-9 SGD PMID 15643063
- ↑ de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 SGD PMID 11746603
- ↑ Lopez-Buesa P, et al. (1998) The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc Natl Acad Sci U S A 95(26):15253-8 SGD PMID 9860955
- ↑ Craig EA, et al. (1993) Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol Rev 57(2):402-14 SGD PMID 8336673
- ↑ Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 SGD PMID 10347213
- ↑ Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105 SGD PMID 1394434
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