Difference between revisions of "YHR034C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YHR034C YHR034C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001076 YHR034C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PIH1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PIH1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr VIII:177992..176958
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|nowrap| Chr VIII:177999..176965
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001076
 
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'''Description of {{PAGENAME}}:''' Protein of unresolved function; may function in protein folding and/or rRNA processing, interacts with a chaperone (Hsp82p), two chromatin remodeling factors (Rvb1p, Rvb2p) and two rRNA processing factors (Rrp43p, Nop58p)<ref name='S000079913'>Jonsson ZO, et al. (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol Cell 16(3):465-77 {{SGDpaper|S000079913}} PMID 15525518</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='S000080660'>Gonzales FA, et al. (2005) Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J Mol Biol 346(2):437-55
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'''Description of YHR034C:''' Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); 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='S000080660'>Gonzales FA, et al. (2005) Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J Mol Biol 346(2):437-55 {{SGDpaper|S000080660}} PMID 15670595</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='S000079913'>Jonsson ZO, et al. (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol Cell 16(3):465-77 {{SGDpaper|S000079913}} PMID 15525518</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|S000080660}} PMID 15670595</ref>
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  {{SGDpaper|S000136091}} PMID 18268103</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 13:05, 6 March 2012

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Systematic name YHR034C
Gene name PIH1
Aliases NOP17
Feature type ORF, Verified
Coordinates Chr VIII:177999..176965
Primary SGDID S000001076


Description of YHR034C: Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); 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][5][6]




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References

See Help:References on how to add references

  1. Jump up 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
  2. Jump up Gonzales FA, et al. (2005) Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J Mol Biol 346(2):437-55 SGD PMID 15670595
  3. Jump up 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
  4. Jump up Jonsson ZO, et al. (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol Cell 16(3):465-77 SGD PMID 15525518
  5. Jump up 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
  6. Jump up 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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