{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,27]],"date-time":"2026-05-27T12:46:47Z","timestamp":1779886007449,"version":"3.53.1"},"reference-count":43,"publisher":"Springer Science and Business Media LLC","issue":"4-5","license":[{"start":{"date-parts":[[2013,7,9]],"date-time":"2013-07-09T00:00:00Z","timestamp":1373328000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Plant Mol Biol"],"published-print":{"date-parts":[[2013,11]]},"DOI":"10.1007\/s11103-013-0100-x","type":"journal-article","created":{"date-parts":[[2013,7,8]],"date-time":"2013-07-08T07:21:23Z","timestamp":1373268083000},"page":"417-432","source":"Crossref","is-referenced-by-count":20,"title":["Molecular characterization of Alr1105 a novel arsenate reductase of the diazotrophic cyanobacterium Anabaena sp. PCC7120 and decoding its role in abiotic stress management in Escherichia coli"],"prefix":"10.1007","volume":"83","author":[{"given":"Sarita","family":"Pandey","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alok K.","family":"Shrivastava","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rashmi","family":"Rai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lal Chand","family":"Rai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2013,7,9]]},"reference":[{"key":"100_CR1","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1007\/s00284-003-4205-3","volume":"48","author":"CR Anderson","year":"2004","unstructured":"Anderson CR, Cook GM (2004) Isolation and characterization of arsenate-reducing bacteria from arsenic-contaminated sites in New Zealand. Curr Microbiol 48:341\u2013347","journal-title":"Curr Microbiol"},{"key":"100_CR2","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1002\/(SICI)1097-0061(199707)13:9<819::AID-YEA142>3.0.CO;2-Y","volume":"13","author":"P Bobrowicz","year":"1997","unstructured":"Bobrowicz P, Wysocki R, Owsianik G, Goffeau A, Ulaszewski S (1997) Isolation of three contiguous genes, ACR1, ACR2, and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Yeast 13:819\u2013828","journal-title":"Yeast"},{"key":"100_CR3","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1128\/jb.177.4.981-986.1995","volume":"177","author":"A Carlin","year":"1995","unstructured":"Carlin A, Shi W, Dey S, Rosen BP (1995) The ars operon of Escherichia coli confers arsenical and antimonial resistance. J Bacteriol 177:981\u2013986","journal-title":"J Bacteriol"},{"key":"100_CR4","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.bbrc.2008.08.129","volume":"376","author":"N Chaurasia","year":"2008","unstructured":"Chaurasia N, Mishra Y, Rai LC (2008) Cloning, expression and analysis of phytochelatin synthase (pcs) gene from Anabaena sp. PCC 7120 offering multiple stress tolerance in Escherichia coli. Biochem Biophys Res Commun 376:225\u2013230","journal-title":"Biochem Biophys Res Commun"},{"key":"100_CR5","doi-asserted-by":"crossref","first-page":"15030","DOI":"10.1016\/S0021-9258(18)66824-3","volume":"261","author":"CM Chen","year":"1986","unstructured":"Chen CM, Misra TK, Silver S, Rosen BP (1986) Nucleotide sequence of the structural gene of an anion pump. The plasmid-encoded arsenical resistance operon. J Biol Chem 261:15030\u201315038","journal-title":"J Biol Chem"},{"key":"100_CR6","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1046\/j.1469-8137.2003.00827.x","volume":"159","author":"OP Dhankher","year":"2003","unstructured":"Dhankher OP, Shastil NA, Rosen BP, Fuhrmann M, Meagher RB (2003) Increased cadmium tolerance and accumulation by plants expressing bacterial arsenate reductase. New Phytol 159:431\u2013441","journal-title":"New Phytol"},{"issue":"6","key":"100_CR8","doi-asserted-by":"crossref","first-page":"e20921","DOI":"10.1371\/journal.pone.0020921","volume":"6","author":"AR Dixit","year":"2011","unstructured":"Dixit AR, Dhankher OP (2011) A novel stress-associated protein \u2018AtSAP10\u2019 from Arabidopsis thaliana confers tolerance to nickel, manganese, zinc, and high temperature stress. PLoS ONE 6(6):e20921. doi: 10.1371\/journal.pone.0020921","journal-title":"PLoS ONE"},{"key":"100_CR9","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1111\/j.1469-8137.2007.02009.x","volume":"174","author":"G-L Duan","year":"2007","unstructured":"Duan G-L, Zhou Y, Yi-Ping T, Mukhopadhyay R, Rosen BP, Zhu Y-G (2007) A CDC25 homologue from rice functions as an arsenate reductase. New Phytol 174:311\u2013321","journal-title":"New Phytol"},{"key":"100_CR10","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1104\/pp.106.084079","volume":"141","author":"DR Ellis","year":"2006","unstructured":"Ellis DR, Gumaelius L, Indriolo E, Pickering IJ, Banks JA, Salt DE (2006) A novel arsenate reductase from the arsenic hyperaccumulating fern Pteris vittata. Plant Physiol 141:1544\u20131554","journal-title":"Plant Physiol"},{"key":"100_CR11","doi-asserted-by":"crossref","first-page":"7288","DOI":"10.1021\/bi00189a033","volume":"33","author":"TB Gladysheva","year":"1994","unstructured":"Gladysheva TB, Oden KL, Rosen BP (1994) Properties of the arsenate reductase of plasmid R773. Biochemistry 33:7288\u20137293","journal-title":"Biochemistry"},{"key":"100_CR12","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1186\/1471-2164-8-350","volume":"8","author":"L Houot","year":"2007","unstructured":"Houot L, Floutier M, Marteyn B, Michaut M, Picciocch A, Legrain P, Aude J-C, Cassier-Chauvat C, Chauvat F (2007) Cadmium triggers an integrated reprogramming of the metabolism of Synechocystis PCC6803, under the control of the Slr1738 regulator. BMC Genomics 8:350","journal-title":"BMC Genomics"},{"key":"100_CR13","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/S0065-2911(02)46003-1","volume":"46","author":"JA Imlay","year":"2002","unstructured":"Imlay JA (2002) How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis. Adv Microb Physiol 46:111\u2013153","journal-title":"Adv Microb Physiol"},{"key":"100_CR14","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/S0968-0004(98)01335-8","volume":"24","author":"CJ Jeffery","year":"1999","unstructured":"Jeffery CJ (1999) Moonlighting proteins. Trends Biochem Sci 24:8\u201311","journal-title":"Trends Biochem Sci"},{"key":"100_CR15","doi-asserted-by":"crossref","first-page":"9474","DOI":"10.1073\/pnas.89.20.9474","volume":"89","author":"G Ji","year":"1992","unstructured":"Ji G, Silver S (1992) Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258. Proc Natl Acad Sci USA 89:9474\u20139478","journal-title":"Proc Natl Acad Sci USA"},{"key":"100_CR16","doi-asserted-by":"crossref","first-page":"7294","DOI":"10.1021\/bi00189a034","volume":"33","author":"G Ji","year":"1994","unstructured":"Ji G, Garber EAE, Armes LG, Chen CM, Fuchs JA, Silver S (1994) Arsenate reductase of Staphylococcus aureus plasmid pI258. Biochemistry 33:7294\u20137299","journal-title":"Biochemistry"},{"key":"100_CR17","doi-asserted-by":"crossref","first-page":"6780","DOI":"10.1128\/JB.185.23.6780-6789.2003","volume":"185","author":"R Li","year":"2003","unstructured":"Li R, Haile JD, Kennelly PJ (2003) An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics. J Bacteriol 185:6780\u20136789","journal-title":"J Bacteriol"},{"key":"100_CR18","doi-asserted-by":"crossref","first-page":"3331","DOI":"10.1128\/JB.186.11.3331-3345.2004","volume":"186","author":"H Li","year":"2004","unstructured":"Li H, Singh AK, McIntyre LM, Sherman LA (2004) Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. Strain PCC 6803. J Bacteriol 186:3331\u20133345","journal-title":"J Bacteriol"},{"key":"100_CR19","doi-asserted-by":"crossref","first-page":"13472","DOI":"10.1021\/bi00041a026","volume":"34","author":"J Liu","year":"1995","unstructured":"Liu J, Gladysheva TB, Lee L, Rosen BP (1995) Identification of an essential cysteine residue in the ArsC arsenate reductase of plasmid R773. Biochemistry 34:13472\u201313476","journal-title":"Biochemistry"},{"key":"100_CR43","doi-asserted-by":"crossref","unstructured":"Lopez-Maury L, Florencio FJ, Reyes JC (2003) Arsenic sensing and resistance system in the cyanobacterium Synechocystis sp. Strain PCC 6803. J Bacteriol 185:5363\u20135371","DOI":"10.1128\/JB.185.18.5363-5371.2003"},{"key":"100_CR20","doi-asserted-by":"crossref","first-page":"3534","DOI":"10.1128\/JB.01798-08","volume":"191","author":"L Lopez-Maury","year":"2009","unstructured":"Lopez-Maury L, Sanchez-Riego AM, Reyes JC, Florencio FJ (2009) The glutathione\/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. Strain PCC 6803. J Bacteriol 191:3534\u20133543","journal-title":"J Bacteriol"},{"key":"100_CR21","doi-asserted-by":"crossref","first-page":"16857","DOI":"10.1021\/bi9911841","volume":"38","author":"J Messens","year":"1999","unstructured":"Messens J, Hayburn G, Desmyter A, Laus G, Wyns L (1999) The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus. Biochemistry 38:16857\u201316865","journal-title":"Biochemistry"},{"key":"100_CR44","doi-asserted-by":"crossref","unstructured":"Messens J,\u00a0 Martins JC, Brosens E, Van Belle K, Jacobs DM, Willem R, Wyns L (2002) Kinetics and active site dynamics of Staphylococcus aureus arsenate reductase. J Biol Inorg Chem 7:146\u2013156","DOI":"10.1007\/s007750100282"},{"key":"100_CR22","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/j.bbrc.2009.02.100","volume":"38","author":"Y Mishra","year":"2009","unstructured":"Mishra Y, Chaurasia N, Rai LC (2009) AhpC (alkyl hydroperoxide reductase) from Anabaena sp. PCC 7120 protects Escherichia coli from multiple abiotic stresses. Biochem Biophys Res Commun 38:606\u2013611","journal-title":"Biochem Biophys Res Commun"},{"key":"100_CR23","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1111\/j.1574-6968.1998.tb13265.x","volume":"168","author":"R Mukhopadhyay","year":"1998","unstructured":"Mukhopadhyay R, Rosen BP (1998) Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase. FEMS Microbiol Lett 168:127\u2013136","journal-title":"FEMS Microbiol Lett"},{"key":"100_CR24","doi-asserted-by":"crossref","first-page":"34738","DOI":"10.1074\/jbc.M103354200","volume":"276","author":"R Mukhopadhyay","year":"2001","unstructured":"Mukhopadhyay R, Rosen BP (2001) The phosphatase C(X)5R motif is required for catalytic activity of Saccharomyces cerevisiae Acr2p arsenate reductase. J Biol Chem 276:34738\u201334742","journal-title":"J Biol Chem"},{"key":"100_CR25","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1289\/ehp.02110s5745","volume":"110","author":"R Mukhopadhyay","year":"2002","unstructured":"Mukhopadhyay R, Rosen BP (2002) Arsenate reductases in prokaryotes and eukaryotes. Environ Health Perspect 110:745\u2013748","journal-title":"Environ Health Perspect"},{"key":"100_CR26","doi-asserted-by":"crossref","first-page":"21149","DOI":"10.1074\/jbc.M910401199","volume":"275","author":"R Mukhopadhyay","year":"2000","unstructured":"Mukhopadhyay R, Shi J, Rosen BP (2000) Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase. J Biol Chem 275:21149\u201321157","journal-title":"J Biol Chem"},{"key":"100_CR27","doi-asserted-by":"crossref","first-page":"4945","DOI":"10.1128\/JB.187.14.4945-4956.2005","volume":"187","author":"L Musumeci","year":"2005","unstructured":"Musumeci L, Bongiorni C, Tautz L, Edwards RA, Osterman A, Perego M, Mustelin T, Bottini N (2005) Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis. J Bacteriol 187:4945\u20134956","journal-title":"J Bacteriol"},{"key":"100_CR28","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.bbrc.2010.02.135","volume":"394","author":"OP Narayan","year":"2010","unstructured":"Narayan OP, Kumari N, Rai LC (2010) Heterologous expression of Anabaena PCC 7120 all3940 (a Dps family gene) protects Escherichia coli from nutrient limitation and abiotic stresses. Biochem Biophys Res Commun 394:163\u2013169","journal-title":"Biochem Biophys Res Commun"},{"key":"100_CR29","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1111\/j.1365-2958.1994.tb01018.x","volume":"12","author":"KL Oden","year":"1994","unstructured":"Oden KL, Gladysheva TB, Rosen BP (1994) Arsenate reduction mediated by the plasmid-encoded ArsC protein is coupled to glutathione. Mol Microbiol 12:301\u2013306","journal-title":"Mol Microbiol"},{"key":"100_CR30","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.tim.2004.12.002","volume":"13","author":"RS Oremland","year":"2005","unstructured":"Oremland RS, Stolz JF (2005) Arsenic, microbes and contaminated aquifers. Trends Microbiol 13:45\u201349","journal-title":"Trends Microbiol"},{"key":"100_CR31","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/j.jprot.2011.10.011","volume":"75","author":"S Pandey","year":"2012","unstructured":"Pandey S, Rai R, Rai LC (2012) Proteomics combines morphological, physiological and biochemical attributes to unravel the survival strategy of Anabaena sp. PCC7120 under arsenic stress. J Proteomics 75:921\u2013937","journal-title":"J Proteomics"},{"key":"100_CR32","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/S1357-2725(96)00109-4","volume":"29","author":"G Ramponi","year":"1997","unstructured":"Ramponi G, Stefani M (1997a) Structural, catalytic, and functional properties of low Mr phosphotyrosine protein phosphatases. Evidence of a long evolutionary history. Int J Biochem Cell Biol 29:279\u2013292","journal-title":"Int J Biochem Cell Biol"},{"key":"100_CR33","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0167-4838(97)00087-3","volume":"1341","author":"G Ramponi","year":"1997","unstructured":"Ramponi G, Stefani M (1997b) Structure and function of the low Mr phosphotyrosine protein phosphatates. Biochim Biophys Acta 1341:137\u2013156","journal-title":"Biochim Biophys Acta"},{"key":"100_CR34","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1099\/00221287-111-1-1","volume":"111","author":"R Rippka","year":"1979","unstructured":"Rippka R, Deruelles J, Waterbury JB, Herdman M, Stanier RY (1979) Generic assignments, strain histories and properties of pure cultures of cyanobacteria. J Gen Microbiol 111:1\u20136","journal-title":"J Gen Microbiol"},{"key":"100_CR35","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/S0968-0004(00)01659-5","volume":"25","author":"F Rusnak","year":"2000","unstructured":"Rusnak F, Reiter T (2000) Sensing electrons: protein phosphatase redox regulation. Trends Biochem Sci 25:527\u2013529","journal-title":"Trends Biochem Sci"},{"key":"100_CR36","volume-title":"Molecular cloning: A laboratory manual","author":"J Sambrook","year":"2001","unstructured":"Sambrook J, Russell DW (2001) Molecular cloning: A laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY"},{"key":"100_CR37","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1128\/AEM.69.1.490-494.2003","volume":"69","author":"S Sauge-Merle","year":"2003","unstructured":"Sauge-Merle S, Cuine\u2032 S, Carrier P, Lecomte-Pradines C, Luu D-T, Peltier G (2003) Enhanced toxic metal accumulation in engineered bacterial cells expressing Arabidopsis thaliana phytochelatin synthase. Appl Environ Microbiol 69:490\u2013494","journal-title":"Appl Environ Microbiol"},{"key":"100_CR38","doi-asserted-by":"crossref","first-page":"36039","DOI":"10.1074\/jbc.274.51.36039","volume":"274","author":"J Shi","year":"1999","unstructured":"Shi J, Vlamis-Gardikas AF, Holmgren A, Rosen BP (1999) Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction. J Biol Chem 274:36039\u201336042","journal-title":"J Biol Chem"},{"key":"100_CR39","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.gene.2012.09.033","volume":"511","author":"AK Shrivastava","year":"2012","unstructured":"Shrivastava AK, Pandey S, Singh PK, Rai S, Rai LC (2012) alr0882 encoding a hypothetical protein of Anabaena PCC7120 protects Escherichia coli from nutrient starvation and abiotic stresses. Gene 511:248\u2013255","journal-title":"Gene"},{"key":"100_CR40","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1007\/s10811-006-9144-5","volume":"19","author":"AK Srivastava","year":"2007","unstructured":"Srivastava AK, Ara A, Bhargava P, Mishra Y, Rai SP, Rai LC (2007) A rapid and cost effective method of genomic DNA isolation from cyanobacterial culture, mat and soil suitable for genomic fingerprinting and community analysis. J Appl Phycol 19:373\u2013382","journal-title":"J Appl Phycol"},{"key":"100_CR41","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1038\/nsb1001-843","volume":"8","author":"I Zegers","year":"2001","unstructured":"Zegers I, Martins JC, Willem R, Wyns L, Messens J (2001) Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty. Nat Struct Biol 8:843\u2013847","journal-title":"Nat Struct Biol"},{"key":"100_CR42","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.molbiopara.2006.03.009","volume":"148","author":"Y Zhou","year":"2006","unstructured":"Zhou Y, Bhattacharjee H, Mukhopadhyay R (2006) Bifunctional role of the leishmanial antimonate reductase LmACR2 as a protein tyrosine phosphatase. Mol Biochem Parasitol 148:161\u2013168","journal-title":"Mol Biochem Parasitol"}],"container-title":["Plant Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11103-013-0100-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11103-013-0100-x\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11103-013-0100-x","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,27]],"date-time":"2022-02-27T16:58:34Z","timestamp":1645981114000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11103-013-0100-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,7,9]]},"references-count":43,"journal-issue":{"issue":"4-5","published-print":{"date-parts":[[2013,11]]}},"alternative-id":["100"],"URL":"https:\/\/doi.org\/10.1007\/s11103-013-0100-x","relation":{},"ISSN":["0167-4412","1573-5028"],"issn-type":[{"value":"0167-4412","type":"print"},{"value":"1573-5028","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,7,9]]}}}