Difference between revisions of "YCR060W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000656 YCR060W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TAH1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TAH1 '' | ||
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| − | '''Description of YCR060W:''' | + | '''Description of YCR060W:''' Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); contains a single TPR domain with at least two TPR motifs; R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II<ref name='S000135237'>Eckert K, et al. (2010) The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J Biol Chem 285(41):31304-12 {{SGDpaper|S000135237}} PMID 20663878</ref><ref name='S000147848'>Jimenez B, et al. (2011) The structure of the minimal tetratricopeptide repeat domain protein Tah1 reveals the mechanism of its interaction with Pih1 and Hsp90. J Biol Chem () {{SGDpaper|S000147848}} PMID 22179618</ref><ref name='S000081009'>Zhao R, et al. (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120(5):715-27 {{SGDpaper|S000081009}} PMID 15766533</ref><ref name='S000136091'>Zhao R, et al. (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J Cell Biol 180(3):563-78 |
| − | {{SGDpaper| | + | {{SGDpaper|S000136091}} PMID 18268103</ref> |
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Latest revision as of 13:05, 6 March 2012
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| Systematic name | YCR060W |
| Gene name | TAH1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr III:224399..224734 |
| Primary SGDID | S000000656 |
Description of YCR060W: Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); contains a single TPR domain with at least two TPR motifs; R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II[1][2][3][4]
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References
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- ↑ Eckert K, et al. (2010) The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J Biol Chem 285(41):31304-12 SGD PMID 20663878
- ↑ Jimenez B, et al. (2011) The structure of the minimal tetratricopeptide repeat domain protein Tah1 reveals the mechanism of its interaction with Pih1 and Hsp90. J Biol Chem () SGD PMID 22179618
- ↑ Zhao R, et al. (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120(5):715-27 SGD PMID 15766533
- ↑ Zhao R, et al. (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J Cell Biol 180(3):563-78 SGD PMID 18268103
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