Difference between revisions of "Phosphatase Subfamily CUT"

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__NOTOC__
 
__NOTOC__
[[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Group_HAD|HAD]]: [[Phosphatase_Family_NagD|NagD]]: [[Phosphatase_Subfamily_Cut|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|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.
  
== Evolution ==
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=== 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.  
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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.
  
== Notes ==
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=== Domain ===
Various Cut genes have been localized to the mitochondria <cite>Barbe, Reinders</cite>. CRCR5, 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. 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 <cite>Youssar</cite>. 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).
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CUT has a single domain, HAD domain.
  
== References ==
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=== 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>. 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).
 +
 
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=== 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

  1. 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 | PubMed ID:28400531 | HubMed [Chen]
  2. 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 | PubMed ID:18029348 | HubMed [Barbe]
  3. 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 | PubMed ID:16823961 | HubMed [Reinders]
  4. 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 | PubMed ID:20186120 | HubMed [Richter]
  5. 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 | PubMed ID:16807008 | HubMed [Youssar]
All Medline abstracts: PubMed | HubMed