Difference between revisions of "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}}"| '''Aliases''' ||''CPN60, MIF4'' | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''CPN60, MIF4, MNA2'' |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]] | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]] | ||
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− | '''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; | + | '''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; phosphorylated<ref name='S000123951'>Reinders J, et al. (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906 {{SGDpaper|S000123951}} PMID 17761666</ref><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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Revision as of 06:21, 26 February 2009
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Systematic name | YLR259C |
Gene name | HSP60 |
Aliases | CPN60, MIF4, MNA2 |
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; phosphorylated[1][2][3][4][5][6]
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References
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- ↑ Reinders J, et al. (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906 SGD PMID 17761666
- ↑ 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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