Difference between revisions of "Phosphatase Subfamily CUT"
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=== Evolution === | === Evolution === | ||
| − | This family is present throughout eukaryotes, mostly single-copy but with several duplications. It is lost from Drosophila but present in other arthropods. | + | This family is present throughout eukaryotes, mostly single-copy but with several duplications <cite>Chen</cite>. It is lost from Drosophila but present in other arthropods. |
=== Domain === | === Domain === | ||
| Line 11: | Line 11: | ||
=== Function === | === Function === | ||
| − | Cut proteins are localized to the mitochondria <cite>Barbe, Reinders</cite>. CECR5, the human Cut gene, has been shown to associate with ICT1, a mitochondrial peptidyl-tRNA hydrolase <cite>Richter</cite> and yeast Cut (YKR070W) genetically interacts with PTH1, a related aminoacyl tRNA hydrolase. A Neurospora homolog, cut-1 is expressed in a light-dependent manner and required for response to osmotic stress <cite>Youssar</cite>. | + | Cut proteins are localized to the mitochondria <cite>Barbe, Reinders</cite>. CECR5, the human Cut gene, has been shown to associate with ICT1, a mitochondrial peptidyl-tRNA hydrolase <cite>Richter</cite> and yeast Cut (YKR070W) genetically interacts with PTH1, a related aminoacyl tRNA hydrolase. A Neurospora homolog, cut-1 is expressed in a light-dependent manner and required for response to osmotic stress <cite>Youssar</cite>. A PhD thesis reports that YKR070W shows phosphatase activity against sugar and glycerol phosphates (https://tspace.library.utoronto.ca/bitstream/1807/19048/1/Kuznetsova_Ekaterina_200911_PhD_thesis.pdf, p129). |
=== References === | === References === | ||
<biblio> | <biblio> | ||
#Barbe pmid=18029348 | #Barbe pmid=18029348 | ||
| + | #Chen pmid=28400531 | ||
#Reinders pmid=16823961 | #Reinders pmid=16823961 | ||
#Richter pmid=20186120 | #Richter pmid=20186120 | ||
#Youssar pmid=16807008 | #Youssar pmid=16807008 | ||
</biblio> | </biblio> | ||
Latest revision as of 00:13, 14 April 2017
Phosphatase Classification: Fold HAD: Superfamily HAD: Family NagD: Subfamily CUT
Cut genes are related to other eukaryotic NagD phosphatases, but have not been shown to have protein phosphatase activity.
Evolution
This family is present throughout eukaryotes, mostly single-copy but with several duplications [1]. It is lost from Drosophila but present in other arthropods.
Domain
CUT has a single domain, HAD domain.
Function
Cut proteins are localized to the mitochondria [2, 3]. CECR5, the human Cut gene, has been shown to associate with ICT1, a mitochondrial peptidyl-tRNA hydrolase [4] and yeast Cut (YKR070W) genetically interacts with PTH1, a related aminoacyl tRNA hydrolase. A Neurospora homolog, cut-1 is expressed in a light-dependent manner and required for response to osmotic stress [5]. A PhD thesis reports that YKR070W shows phosphatase activity against sugar and glycerol phosphates (https://tspace.library.utoronto.ca/bitstream/1807/19048/1/Kuznetsova_Ekaterina_200911_PhD_thesis.pdf, p129).
References
- Chen MJ, Dixon JE, and Manning G. Genomics and evolution of protein phosphatases. Sci Signal. 2017 Apr 11;10(474). DOI:10.1126/scisignal.aag1796 |
- Barbe L, Lundberg E, Oksvold P, Stenius A, Lewin E, Björling E, Asplund A, Pontén F, Brismar H, Uhlén M, and Andersson-Svahn H. Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics. 2008 Mar;7(3):499-508. DOI:10.1074/mcp.M700325-MCP200 |
- Reinders J, Zahedi RP, Pfanner N, Meisinger C, and Sickmann A. Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res. 2006 Jul;5(7):1543-54. DOI:10.1021/pr050477f |
- Richter R, Rorbach J, Pajak A, Smith PM, Wessels HJ, Huynen MA, Smeitink JA, Lightowlers RN, and Chrzanowska-Lightowlers ZM. A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome. EMBO J. 2010 Mar 17;29(6):1116-25. DOI:10.1038/emboj.2010.14 |
- Youssar L and Avalos J. Light-dependent regulation of the gene cut-1 of Neurospora, involved in the osmotic stress response. Fungal Genet Biol. 2006 Nov;43(11):752-63. DOI:10.1016/j.fgb.2006.05.003 |
