Difference between revisions of "YFL016C"

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'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71 {{SGDpaper|S000044393}} PMID 8943361</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59
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'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59 {{SGDpaper|S000048831}} PMID 8168133</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71
  {{SGDpaper|S000048831}} PMID 8168133</ref>
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  {{SGDpaper|S000044393}} PMID 8943361</ref>
 
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Revision as of 14:05, 25 February 2010

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Systematic name YFL016C
Gene name MDJ1
Aliases
Feature type ORF, Verified
Coordinates Chr VI:106230..104695
Primary SGDID S000001878


Description of YFL016C: Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones[1][2][3][4]




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References

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  1. Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 SGD PMID 9973563
  2. Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59 SGD PMID 8168133
  3. Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 SGD PMID 7957078
  4. Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71 SGD PMID 8943361

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