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
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