Difference between revisions of "Phosphatase Subfamily Acr2"
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Prokaryotes and eukaryotes use arsenate reductases of distinct folds. ''E. coli'' uses ArsC, which belongs to [[Phosphatase_Superfamily_Cys-based_III|Superfamily Cys-based III]], the same as [[Phosphatase_Family_LMWPTP|LMWPTP]] and [[Phosphatase_Family_SSU72|SSU72]]. Eukaryotes, particularly fungi, plants and protists, use ACR2 which have the same fold as [[Phosphatase_Family_CDC25|CDC25]] <cite>yeo09</cite>. | Prokaryotes and eukaryotes use arsenate reductases of distinct folds. ''E. coli'' uses ArsC, which belongs to [[Phosphatase_Superfamily_Cys-based_III|Superfamily Cys-based III]], the same as [[Phosphatase_Family_LMWPTP|LMWPTP]] and [[Phosphatase_Family_SSU72|SSU72]]. Eukaryotes, particularly fungi, plants and protists, use ACR2 which have the same fold as [[Phosphatase_Family_CDC25|CDC25]] <cite>yeo09</cite>. | ||
| − | === Arc2 | + | === Arc2 in eukaryotes === |
| − | ''Saccharomyces cerevisiae''. Overexpressed in ''E. coli'', the ACR2 gene of ''Saccharomyces cerevisiae'' | + | ''Saccharomyces cerevisiae''. Overexpressed in ''E. coli'', [http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006404 ARR2], the ACR2 gene of ''Saccharomyces cerevisiae'', was shown to exhibit arsenate reductase activity and complement the arsenate-sensitive phenotype of an ArsC deletion in ''E. coli'' <cite>yeast98 yeast00 yeo09</cite>. The Cx5R motif is required for its catalytic activity as arsenate reductase <cite>yeast01</cite>. |
| − | + | ''Pteris vittata'' (fern). The ACR2 of "Pteris vittata" (PvACR2) can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (''Saccharomyces cerevisiae'') lacking the arsenate reductase gene ACR2 <cite>fern06</cite>. However, PvACR2 is unique in that the arginine of catalytic motif Cx5R, previously shown to be essential for phosphatase and reductase activity, is replaced with a serine. | |
=== Reference === | === Reference === | ||
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#yeast98 pmid=9812373 | #yeast98 pmid=9812373 | ||
#yeast00 pmid=10801893 | #yeast00 pmid=10801893 | ||
| + | #yeast01 pmid=11461905 | ||
#fern06 pmid=16766666 | #fern06 pmid=16766666 | ||
</biblio> | </biblio> | ||
Revision as of 16:22, 27 May 2014
Phosphatase Classification: Superfamily Cys-based II: Family CDC25: Subfamily Acr2
Prokaryotes and eukaryotes use arsenate reductases of distinct folds. E. coli uses ArsC, which belongs to Superfamily Cys-based III, the same as LMWPTP and SSU72. Eukaryotes, particularly fungi, plants and protists, use ACR2 which have the same fold as CDC25 [1].
Arc2 in eukaryotes
Saccharomyces cerevisiae. Overexpressed in E. coli, ARR2, the ACR2 gene of Saccharomyces cerevisiae, was shown to exhibit arsenate reductase activity and complement the arsenate-sensitive phenotype of an ArsC deletion in E. coli [1, 2, 3]. The Cx5R motif is required for its catalytic activity as arsenate reductase [4].
Pteris vittata (fern). The ACR2 of "Pteris vittata" (PvACR2) can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (Saccharomyces cerevisiae) lacking the arsenate reductase gene ACR2 [5]. However, PvACR2 is unique in that the arginine of catalytic motif Cx5R, previously shown to be essential for phosphatase and reductase activity, is replaced with a serine.
Reference
- Yeo HK and Lee JY. Crystal structure of Saccharomyces cerevisiae Ygr203w, a homolog of single-domain rhodanese and Cdc25 phosphatase catalytic domain. Proteins. 2009 Aug 1;76(2):520-4. DOI:10.1002/prot.22420 |
- Mukhopadhyay R and Rosen BP. Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase. FEMS Microbiol Lett. 1998 Nov 1;168(1):127-36. DOI:10.1111/j.1574-6968.1998.tb13265.x |
- Mukhopadhyay R, Shi J, and Rosen BP. Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase. J Biol Chem. 2000 Jul 14;275(28):21149-57. DOI:10.1074/jbc.M910401199 |
- Mukhopadhyay R and Rosen BP. The phosphatase C(X)5R motif is required for catalytic activity of the Saccharomyces cerevisiae Acr2p arsenate reductase. J Biol Chem. 2001 Sep 14;276(37):34738-42. DOI:10.1074/jbc.M103354200 |
- Ellis DR, Gumaelius L, Indriolo E, Pickering IJ, Banks JA, and Salt DE. A novel arsenate reductase from the arsenic hyperaccumulating fern Pteris vittata. Plant Physiol. 2006 Aug;141(4):1544-54. DOI:10.1104/pp.106.084079 |
