Difference between revisions of "YOL021C"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
Line 18: Line 18:
 
|}
 
|}
 
<br>
 
<br>
'''Description of YOL021C:''' Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3<ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90 {{SGDpaper|S000054682}} PMID 9562621</ref><ref name='S000129101'>Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 {{SGDpaper|S000129101}} PMID 19060898</ref><ref name='S000120270'>Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 {{SGDpaper|S000120270}} PMID 17174896</ref><ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000125981'>Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 {{SGDpaper|S000125981}} PMID 18374646</ref><ref name='S000128588'>Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 {{SGDpaper|S000128588}} PMID 19060886</ref><ref name='S000128894'>Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37(4):1127-40
+
'''Description of YOL021C:''' Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3<ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000128588'>Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 {{SGDpaper|S000128588}} PMID 19060886</ref><ref name='S000120270'>Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 {{SGDpaper|S000120270}} PMID 17174896</ref><ref name='S000125981'>Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 {{SGDpaper|S000125981}} PMID 18374646</ref><ref name='S000129101'>Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 {{SGDpaper|S000129101}} PMID 19060898</ref><ref name='S000128894'>Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37(4):1127-40 {{SGDpaper|S000128894}} PMID 19129231</ref><ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90
  {{SGDpaper|S000128894}} PMID 19129231</ref>
+
  {{SGDpaper|S000054682}} PMID 9562621</ref>
 
<br>
 
<br>
 
<br>
 
<br>

Revision as of 14:05, 25 February 2010

Share your knowledge...Edit this entry! <protect>

Systematic name YOL021C
Gene name DIS3
Aliases RRP44
Feature type ORF, Verified
Coordinates Chr XV:285427..282422
Primary SGDID S000005381


Description of YOL021C: Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3[1][2][3][4][5][6][7]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!





<protect>

References

See Help:References on how to add references

  1. Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 SGD PMID 17173052
  2. Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 SGD PMID 19060886
  3. Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 SGD PMID 17174896
  4. Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 SGD PMID 18374646
  5. Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 SGD PMID 19060898
  6. Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37(4):1127-40 SGD PMID 19129231
  7. Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90 SGD PMID 9562621

See Help:Categories on how to add the wiki page for this gene to a Category </protect>