Difference between revisions of "Phosphatase Subfamily Acr2"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_II|Superfamily Cys-based II]]: [[Phosphatase_Family_CDC25|Family CDC25]]: [[Subfamily_Acr2|Subfamily Acr2]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_II|Superfamily Cys-based II]]: [[Phosphatase_Family_CDC25|Family CDC25]]: [[Subfamily_Acr2|Subfamily Acr2]] | ||
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| + | === Acr2, CDC25 phosphatase or arsenate reductase in eukaryotes or both? === | ||
| + | Acr2 is found in fungi, plants and protists, but not in animals. It is close to CDC25 in both sequence and structure. Yeast has both CDC25 and Acr2. They are generally regarded as tyrosine phosphatase involved in cell cycle and arsenate reductase, respectively. However, in plants, Acr2 is the only gene close to CDC25, and it is controversial whether it functions as both phosphatase and arsenate reductase in vivo, if not, what its major function is (see below). | ||
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, may use ACR2 which have the same fold as [[Phosphatase_Family_CDC25|CDC25]] <cite>yeo09</cite>. However, knocking out ACR2 does not affect arsenic redox status in ''Arabidopsis thaliana'' and ''Saccharomyces cerevisiae'' , which implies the existence of other arsenate reductase(s) in plants and yeast <cite>atha-ar-12</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, may use ACR2 which have the same fold as [[Phosphatase_Family_CDC25|CDC25]] <cite>yeo09</cite>. However, knocking out ACR2 does not affect arsenic redox status in ''Arabidopsis thaliana'' and ''Saccharomyces cerevisiae'' , which implies the existence of other arsenate reductase(s) in plants and yeast <cite>atha-ar-12</cite>. | ||
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''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>. | ''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>. | ||
| − | ''Arabidopsis thaliana''. Acr2 of ''Arabidopsis thaliana'' was initially characterized as a phosphatase, given the evidences: i) protein structure solved by NMR <cite>atha-phosphatase-04</cite>, ii) recombinant expression in E. coli shows tyrosine phosphatase activity towards artificial substrate <cite>atha-phosphatase-04b</cite>, and iii) overexpression in fission yeast function suggests it is a mitotic accelerator <cite>atha-phosphatase-05</cite>. It has been suggested to play a role in arsenate reduction <cite>atha-ar-06 atha-ar-06b fern05</cite>. However, knocking out ACR2 does not affect arsenic redox status in ''Arabidopsis thaliana'' and ''Saccharomyces cerevisiae'' <cite>atha-ar-12</cite>. | + | ''Arabidopsis thaliana''. [http://www.ncbi.nlm.nih.gov/gene/831832 Acr2] of ''Arabidopsis thaliana'' was initially characterized as a phosphatase, given the evidences: i) protein structure solved by NMR <cite>atha-phosphatase-04</cite>, ii) recombinant expression in E. coli shows tyrosine phosphatase activity towards artificial substrate <cite>atha-phosphatase-04b</cite>, and iii) overexpression in fission yeast function suggests it is a mitotic accelerator <cite>atha-phosphatase-05</cite>. It has been suggested to play a role in arsenate reduction <cite>atha-ar-06 atha-ar-06b fern05</cite>. However, knocking out ACR2 does not affect arsenic redox status in ''Arabidopsis thaliana'' and ''Saccharomyces cerevisiae'' <cite>atha-ar-12</cite>. |
''Oryza sativa'' (rice). Rice has two Acr2s, which can complement the arsenate-sensitive phenotype of an ArsC deletion in ''E. coli'' at different levels<cite>duan-07</cite>. The two genes not only reduce arsenate to arsenite in vitro, but also exhibit phosphatase activity. Mutagenesis of cysteine residues in the catalytic motif CX5R led to nearly complete loss of both phosphatase and arsenate reductase activities <cite>duan-07</cite>. | ''Oryza sativa'' (rice). Rice has two Acr2s, which can complement the arsenate-sensitive phenotype of an ArsC deletion in ''E. coli'' at different levels<cite>duan-07</cite>. The two genes not only reduce arsenate to arsenite in vitro, but also exhibit phosphatase activity. Mutagenesis of cysteine residues in the catalytic motif CX5R led to nearly complete loss of both phosphatase and arsenate reductase activities <cite>duan-07</cite>. | ||
| − | ''Pteris vittata'' (fern). | + | ''Pteris vittata'' (fern). "Pteris vittata" has a single ACR2 (PvACR2). It product protein can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (''Saccharomyces cerevisiae'') lacking the arsenate reductase gene ACR2 <cite>fern05 fern06</cite>. Interestingly, PvACR2 has replaced arginine with serine at the catalytic motif Cx5R, previously shown to be essential for phosphatase and reductase activity. While Acr2s in ''Arabidopsis thaliana'' and rice show both arsenate reductase and phosphatase activities, PvACR2 only shows arsenate reductase activity <cite>fern06</cite>. |
''Chlamydomonas reinhardtii'' (green alga). ''Chlamydomonas reinhardtii'' has two Acr2s. One of them complement the arsenate-sensitive phenotype of an ArsC deletion in ''E. coli'' <cite>green-alga-11</cite>. | ''Chlamydomonas reinhardtii'' (green alga). ''Chlamydomonas reinhardtii'' has two Acr2s. One of them complement the arsenate-sensitive phenotype of an ArsC deletion in ''E. coli'' <cite>green-alga-11</cite>. | ||
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=== Reference === | === Reference === | ||
Revision as of 17:51, 27 May 2014
Phosphatase Classification: Superfamily Cys-based II: Family CDC25: Subfamily Acr2
Acr2, CDC25 phosphatase or arsenate reductase in eukaryotes or both?
Acr2 is found in fungi, plants and protists, but not in animals. It is close to CDC25 in both sequence and structure. Yeast has both CDC25 and Acr2. They are generally regarded as tyrosine phosphatase involved in cell cycle and arsenate reductase, respectively. However, in plants, Acr2 is the only gene close to CDC25, and it is controversial whether it functions as both phosphatase and arsenate reductase in vivo, if not, what its major function is (see below).
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, may use ACR2 which have the same fold as CDC25 [1]. However, knocking out ACR2 does not affect arsenic redox status in Arabidopsis thaliana and Saccharomyces cerevisiae , which implies the existence of other arsenate reductase(s) in plants and yeast [2].
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, 3, 4]. The Cx5R motif is required for its catalytic activity as arsenate reductase [5].
Arabidopsis thaliana. Acr2 of Arabidopsis thaliana was initially characterized as a phosphatase, given the evidences: i) protein structure solved by NMR [6], ii) recombinant expression in E. coli shows tyrosine phosphatase activity towards artificial substrate [7], and iii) overexpression in fission yeast function suggests it is a mitotic accelerator [8]. It has been suggested to play a role in arsenate reduction [9, 10, 11]. However, knocking out ACR2 does not affect arsenic redox status in Arabidopsis thaliana and Saccharomyces cerevisiae [2].
Oryza sativa (rice). Rice has two Acr2s, which can complement the arsenate-sensitive phenotype of an ArsC deletion in E. coli at different levels[12]. The two genes not only reduce arsenate to arsenite in vitro, but also exhibit phosphatase activity. Mutagenesis of cysteine residues in the catalytic motif CX5R led to nearly complete loss of both phosphatase and arsenate reductase activities [12].
Pteris vittata (fern). "Pteris vittata" has a single ACR2 (PvACR2). It product protein can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (Saccharomyces cerevisiae) lacking the arsenate reductase gene ACR2 [11, 13]. Interestingly, PvACR2 has replaced arginine with serine at the catalytic motif Cx5R, previously shown to be essential for phosphatase and reductase activity. While Acr2s in Arabidopsis thaliana and rice show both arsenate reductase and phosphatase activities, PvACR2 only shows arsenate reductase activity [13].
Chlamydomonas reinhardtii (green alga). Chlamydomonas reinhardtii has two Acr2s. One of them complement the arsenate-sensitive phenotype of an ArsC deletion in E. coli [14].
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 |
- Liu W, Schat H, Bliek M, Chen Y, McGrath SP, George G, Salt DE, and Zhao FJ. Knocking out ACR2 does not affect arsenic redox status in Arabidopsis thaliana: implications for as detoxification and accumulation in plants. PLoS One. 2012;7(8):e42408. DOI:10.1371/journal.pone.0042408 |
- 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 |
- Landrieu I, da Costa M, De Veylder L, Dewitte F, Vandepoele K, Hassan S, Wieruszeski JM, Corellou F, Faure JD, Van Montagu M, Inzé D, and Lippens G. A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13380-5. DOI:10.1073/pnas.0405248101 |
- Landrieu I, da Costa M, De Veylder L, Dewitte F, Vandepoele K, Hassan S, Wieruszeski JM, Corellou F, Faure JD, Van Montagu M, Inzé D, and Lippens G. A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13380-5. DOI:10.1073/pnas.0405248101 |
- Sorrell DA, Chrimes D, Dickinson JR, Rogers HJ, and Francis D. The Arabidopsis CDC25 induces a short cell length when overexpressed in fission yeast: evidence for cell cycle function. New Phytol. 2005 Feb;165(2):425-8. DOI:10.1111/j.1469-8137.2004.01288.x |
- Bleeker PM, Hakvoort HW, Bliek M, Souer E, and Schat H. Enhanced arsenate reduction by a CDC25-like tyrosine phosphatase explains increased phytochelatin accumulation in arsenate-tolerant Holcus lanatus. Plant J. 2006 Mar;45(6):917-29. DOI:10.1111/j.1365-313X.2005.02651.x |
- Dhankher OP, Rosen BP, McKinney EC, and Meagher RB. Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2). Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5413-8. DOI:10.1073/pnas.0509770102 |
- Duan GL, Zhu YG, Tong YP, Cai C, and Kneer R. Characterization of arsenate reductase in the extract of roots and fronds of Chinese brake fern, an arsenic hyperaccumulator. Plant Physiol. 2005 May;138(1):461-9. DOI:10.1104/pp.104.057422 |
- Duan GL, Zhou Y, Tong YP, Mukhopadhyay R, Rosen BP, and Zhu YG. A CDC25 homologue from rice functions as an arsenate reductase. New Phytol. 2007;174(2):311-321. DOI:10.1111/j.1469-8137.2007.02009.x |
- 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 |
- Yin X, Wang L, Duan G, and Sun G. Characterization of arsenate transformation and identification of arsenate reductase in a green alga Chlamydomonas reinhardtii. J Environ Sci (China). 2011;23(7):1186-93. DOI:10.1016/s1001-0742(10)60492-5 |
- Boudolf V, Inzé D, and De Veylder L. What if higher plants lack a CDC25 phosphatase?. Trends Plant Sci. 2006 Oct;11(10):474-9. DOI:10.1016/j.tplants.2006.08.009 |
