Difference between revisions of "Phosphatase Subfamily CUT"
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| − | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_CUT|CUT]] | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_CUT|Subfamily CUT]] |
Cut genes are related to other eukaryotic NagD phosphatases, but have not been shown to have protein phosphatase activity. | Cut genes are related to other eukaryotic NagD phosphatases, but have not been shown to have protein phosphatase activity. | ||
Revision as of 04:59, 9 March 2015
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 (while it is absent from fruit fly, it is found in other arthropods). It has a single copy in mammals, 2 copies in chicken (but single copy in turkey), 2-3 copies in fishes, 2-3 copies in fungi, 2-3 copies Discicristates, and even 6 copies in Tetrahymena. Phylogenetic tree shows these copies are due to different duplication events.
Domain
CUT has a single domain, HAD domain.
Function
Various Cut genes have been localized to the mitochondria [1, 2]. CECR5, the human Cut gene, has been shown to associate with ICT1, a mitochondrial peptidyl-tRNA hydrolase [3] and yeast Cut (YKR070W) genetically interacts with PTH1, a related aminoacyl tRNA hydrolase. The Drosophila homolog, CG6094 was also seen to interact with NHP2, a protein associated with ribosome biogenesis and telomeres. A Neurospora homolog, cut-1 is expressed in a light-dependent manner and required for response to osmotic stress [4]. An 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
- 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 |
