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]] | ||
| − | 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, 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>. |
=== Arc2 in eukaryotes === | === Arc2 in eukaryotes === | ||
''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>. | ||
| − | ''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. | + | ''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>. |
| + | |||
| + | ''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>fern05 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. | ||
| + | |||
| + | ''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> | ||
=== Reference === | === Reference === | ||
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#yeast00 pmid=10801893 | #yeast00 pmid=10801893 | ||
#yeast01 pmid=11461905 | #yeast01 pmid=11461905 | ||
| + | #atha-phosphatase-04 pmid=15329414 | ||
| + | #atha-phosphatase-04b pmid=15329414 | ||
| + | #atha-phosphatase-05 pmid=15720653 | ||
| + | #atha-ar-06 pmid=16507083 | ||
| + | #atha-ar-06b pmid=16567632 | ||
| + | #atha-ar-12 pmid=22879969 | ||
| + | #fern05 pmid=15834011 | ||
#fern06 pmid=16766666 | #fern06 pmid=16766666 | ||
| + | #green-alga-11 pmid=22125913 | ||
</biblio> | </biblio> | ||
Revision as of 17:16, 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, 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].
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, 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].
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 [11, 12]. 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.
Chlamydomonas reinhardtii (green alga). Chlamydomonas reinhardtii has two Acr2s. One of them complement the arsenate-sensitive phenotype of an ArsC deletion in E. coli [13]
Reference
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