Difference between revisions of "YLR259C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004249 YLR259C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP60 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP60 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XII:665004..663286 | |nowrap| Chr XII:665004..663286 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004249 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YLR259C:''' Tetradecameric mitochondrial chaperonin required for ATP-dependent folding of precursor polypeptides and complex assembly; prevents aggregation and mediates protein refolding after heat shock; role in mtDNA transmission; similarity to groEL<ref name='S000074325'>Kaufman BA, et al. (2003) A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae. J Cell Biol 163(3):457-61 {{SGDpaper|S000074325}} PMID 14597775</ref><ref name='S000052415'>Cheng MY, et al. (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337(6208):620-5 {{SGDpaper|S000052415}} PMID 2645524</ref><ref name='S000051994'>Reading DS, et al. (1989) Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337(6208):655-9 {{SGDpaper|S000051994}} PMID 2563898</ref><ref name='S000049416'>Koll H, et al. (1992) Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68(6):1163-75 {{SGDpaper|S000049416}} PMID 1347713</ref><ref name='S000043162'>Cheng MY, et al. (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348(6300):455-8 |
{{SGDpaper|S000043162}} PMID 1978929</ref> | {{SGDpaper|S000043162}} PMID 1978929</ref> | ||
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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<protect> | <protect> | ||
Revision as of 07:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YLR259C |
| Gene name | HSP60 |
| Aliases | CPN60, MIF4 |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:665004..663286 |
| Primary SGDID | S000004249 |
Description of YLR259C: Tetradecameric mitochondrial chaperonin required for ATP-dependent folding of precursor polypeptides and complex assembly; prevents aggregation and mediates protein refolding after heat shock; role in mtDNA transmission; similarity to groEL[1][2][3][4][5]
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References
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- ↑ Kaufman BA, et al. (2003) A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae. J Cell Biol 163(3):457-61 SGD PMID 14597775
- ↑ Cheng MY, et al. (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337(6208):620-5 SGD PMID 2645524
- ↑ Reading DS, et al. (1989) Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337(6208):655-9 SGD PMID 2563898
- ↑ Koll H, et al. (1992) Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68(6):1163-75 SGD PMID 1347713
- ↑ Cheng MY, et al. (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348(6300):455-8 SGD PMID 1978929
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