{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T15:38:56Z","timestamp":1790869136454,"version":"4.1.0"},"reference-count":44,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2008,8,1]],"date-time":"2008-08-01T00:00:00Z","timestamp":1217548800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2008,8,1]],"date-time":"2008-08-01T00:00:00Z","timestamp":1217548800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","award":["18780073"],"award-info":[{"award-number":["18780073"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2008,8]]},"DOI":"10.1016\/j.bbrc.2008.05.019","type":"journal-article","created":{"date-parts":[[2008,5,14]],"date-time":"2008-05-14T04:19:29Z","timestamp":1210738769000},"page":"407-411","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":16,"title":["The iscS gene deficiency affects the expression of pyrimidine metabolism genes"],"prefix":"10.1016","volume":"372","author":[{"given":"Hisaaki","family":"Mihara","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryota","family":"Hidese","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masahiro","family":"Yamane","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatsuo","family":"Kurihara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nobuyoshi","family":"Esaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2008.05.019_bib1","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1007\/s00253-002-1107-4","article-title":"Bacterial cysteine desulfurases: their function and mechanisms","volume":"60","author":"Mihara","year":"2002","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib2","doi-asserted-by":"crossref","unstructured":"M. Fontecave, S. Ollagnier-de-Choudens, Iron\u2013sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer, Arch. Biochem. Biophys. (2007), doi:10.1016\/j.abb.2007.12.014.","DOI":"10.1016\/j.abb.2007.12.014"},{"key":"10.1016\/j.bbrc.2008.05.019_bib3","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/S1367-5931(03)00021-8","article-title":"Formation of iron\u2013sulfur clusters in bacteria: an emerging field in bioinorganic chemistry","volume":"7","author":"Frazzon","year":"2003","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib4","doi-asserted-by":"crossref","first-page":"13264","DOI":"10.1074\/jbc.273.21.13264","article-title":"Assembly of iron\u2013sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii","volume":"273","author":"Zheng","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib5","doi-asserted-by":"crossref","first-page":"16068","DOI":"10.1016\/S0021-9258(18)48580-8","article-title":"Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe\u2013S cluster of dihydroxy-acid dehydratase","volume":"271","author":"Flint","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib6","doi-asserted-by":"crossref","first-page":"3307","DOI":"10.1128\/JB.181.10.3307-3309.1999","article-title":"SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe\u20132S] FhuF protein in Escherichia coli","volume":"181","author":"Patzer","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib7","doi-asserted-by":"crossref","first-page":"14768","DOI":"10.1074\/jbc.274.21.14768","article-title":"A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies","volume":"274","author":"Mihara","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib8","doi-asserted-by":"crossref","first-page":"22417","DOI":"10.1074\/jbc.272.36.22417","article-title":"Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme","volume":"272","author":"Mihara","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib9","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1093\/oxfordjournals.jbchem.a002963","article-title":"Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron\u2013sulfur proteins","volume":"130","author":"Tokumoto","year":"2001","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib10","doi-asserted-by":"crossref","first-page":"9009","DOI":"10.1073\/pnas.160261497","article-title":"The cysteine desulfurase, IscS, has a major role in in vivo Fe\u2013S cluster formation in Escherichia coli","volume":"97","author":"Schwartz","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2008.05.019_bib11","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1093\/oxfordjournals.jbchem.a022535","article-title":"Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe\u2013S clusters in Escherichia coli","volume":"126","author":"Takahashi","year":"1999","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib12","doi-asserted-by":"crossref","first-page":"28380","DOI":"10.1074\/jbc.C200365200","article-title":"A third bacterial system for the assembly of iron\u2013sulfur clusters with homologs in archaea and plastids","volume":"277","author":"Takahashi","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib13","doi-asserted-by":"crossref","first-page":"20096","DOI":"10.1074\/jbc.M002680200","article-title":"The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD","volume":"275","author":"Lauhon","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib14","doi-asserted-by":"crossref","first-page":"2879","DOI":"10.1128\/JB.182.10.2879-2885.2000","article-title":"Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli","volume":"182","author":"Kiyasu","year":"2000","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib15","doi-asserted-by":"crossref","first-page":"6820","DOI":"10.1128\/JB.184.24.6820-6829.2002","article-title":"Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli","volume":"184","author":"Lauhon","year":"2002","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib16","doi-asserted-by":"crossref","first-page":"16561","DOI":"10.1021\/bi991119r","article-title":"IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA","volume":"38","author":"Kambampati","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2008.05.019_bib17","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1021\/bi026536+","article-title":"MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli","volume":"42","author":"Kambampati","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2008.05.019_bib18","doi-asserted-by":"crossref","first-page":"6679","DOI":"10.1073\/pnas.102176099","article-title":"The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H","volume":"99","author":"Mihara","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2008.05.019_bib19","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S0968-0004(97)01068-2","article-title":"Redox signal transduction via iron\u2013sulfur clusters in the SoxR transcription activator","volume":"22","author":"Hidalgo","year":"1997","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbrc.2008.05.019_bib20","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1111\/j.1365-2958.2006.05160.x","article-title":"IscR-dependent gene expression links iron\u2013sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli","volume":"60","author":"Giel","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib21","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/S0168-6445(03)00066-4","article-title":"Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs","volume":"27","author":"Korner","year":"2003","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.bbrc.2008.05.019_bib22","doi-asserted-by":"crossref","first-page":"3157","DOI":"10.1099\/00221287-146-12-3157","article-title":"YeiL, the third member of the CRP-FNR family in Escherichia coli","volume":"146","author":"Anjum","year":"2000","journal-title":"Microbiology"},{"key":"10.1016\/j.bbrc.2008.05.019_bib23","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/0003-2697(88)90106-6","article-title":"A stain for iron-containing proteins sensitive to nanogram levels of iron","volume":"170","author":"Kuo","year":"1988","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib24","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib25","doi-asserted-by":"crossref","first-page":"2444","DOI":"10.1073\/pnas.85.8.2444","article-title":"Improved tools for biological sequence comparison","volume":"85","author":"Pearson","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2008.05.019_bib26","doi-asserted-by":"crossref","first-page":"6741","DOI":"10.1093\/nar\/17.16.6741","article-title":"Nucleotide sequence of the Escherichia coli uridine phosphorylase (udp) gene","volume":"17","author":"Walton","year":"1989","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2008.05.019_bib27","doi-asserted-by":"crossref","first-page":"4168","DOI":"10.1021\/bi00132a003","article-title":"Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene","volume":"31","author":"Yang","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2008.05.019_bib28","series-title":"Escherichia coli and Salmonella: Cellular and Molecular Biology","first-page":"580","article-title":"Biosynthesis and conversions of pyrimidines","author":"Neuhard","year":"1996"},{"key":"10.1016\/j.bbrc.2008.05.019_bib29","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/0005-2744(76)90283-7","article-title":"Uridine phosphorylase from Escherichia coli. Kinetic properties and mechanism","volume":"429","author":"Krenitsky","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbrc.2008.05.019_bib30","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1093\/oxfordjournals.jbchem.a130305","article-title":"The purification and properties of cytidine deaminase from Escherichia coli","volume":"74","author":"Hosono","year":"1973","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib31","doi-asserted-by":"crossref","first-page":"7561","DOI":"10.1016\/S0021-9258(19)45812-2","article-title":"Cytidine deaminase from Escherichia coli. Purification, properties and inhibition by the potential transition state analog 3,4,5,6-tetrahydrouridine","volume":"246","author":"Cohen","year":"1971","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib32","doi-asserted-by":"crossref","first-page":"3306","DOI":"10.1002\/elps.200500912","article-title":"A complexomic study of Escherichia coli using two-dimensional blue native\/SDS\u2013polyacrylamide gel electrophoresis","volume":"27","author":"Lasserre","year":"2006","journal-title":"Electrophoresis"},{"key":"10.1016\/j.bbrc.2008.05.019_bib33","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1093\/emboj\/20.4.650","article-title":"Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti-cancer drug 5-fluorouracil","volume":"20","author":"Dobritzsch","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.bbrc.2008.05.019_bib34","doi-asserted-by":"crossref","first-page":"17598","DOI":"10.1021\/bi9815997","article-title":"Porcine recombinant dihydropyrimidine dehydrogenase: comparison of the spectroscopic and catalytic properties of the wild-type and C671A mutant enzymes","volume":"37","author":"Rosenbaum","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2008.05.019_bib35","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.bbapap.2004.06.009","article-title":"Dihydropyrimidine dehydrogenase: a flavoprotein with four iron\u2013sulfur clusters","volume":"1701","author":"Schnackerz","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbrc.2008.05.019_bib36","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/S0021-9258(18)70749-7","article-title":"Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase","volume":"227","author":"Campbell","year":"1957","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib37","doi-asserted-by":"crossref","first-page":"16010","DOI":"10.1074\/jbc.274.23.16010","article-title":"Role of multiple CytR binding sites on cooperativity, competition, and induction at the Escherichia coliudp promoter","volume":"274","author":"Gavigan","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2008.05.019_bib38","doi-asserted-by":"crossref","first-page":"1614","DOI":"10.1128\/jb.178.6.1614-1622.1996","article-title":"Analysis of CRP\u2013CytR interactions at the Escherichia coliudp promoter","volume":"178","author":"Brikun","year":"1996","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib39","doi-asserted-by":"crossref","first-page":"3635","DOI":"10.1002\/j.1460-2075.1992.tb05448.x","article-title":"The cAMP-CRP\/CytR nucleoprotein complex in Escherichia coli: two pairs of closely linked binding sites for the cAMP-CRP activator complex are involved in combinatorial regulation of the cdd promoter","volume":"11","author":"Holst","year":"1992","journal-title":"EMBO J."},{"key":"10.1016\/j.bbrc.2008.05.019_bib40","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.1111\/j.1365-2958.1989.tb00120.x","article-title":"CRP\/cAMP- and CytR-regulated promoters in Escherichia coli K12: the cdd promoter","volume":"3","author":"Valentin-Hansen","year":"1989","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib41","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1046\/j.1365-2958.1996.5341056.x","article-title":"A flexible partnership: the CytR anti-activator and the cAMP-CRP activator protein, comrades in transcription control","volume":"20","author":"Valentin-Hansen","year":"1996","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib42","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1126\/science.6372090","article-title":"Cyclic AMP receptor protein: role in transcription activation","volume":"224","author":"de Crombrugghe","year":"1984","journal-title":"Science"},{"key":"10.1016\/j.bbrc.2008.05.019_bib43","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/0022-2836(88)90482-2","article-title":"Selection of DNA binding sites by regulatory proteins. II. The binding specificity of cyclic AMP receptor protein to recognition sites","volume":"200","author":"Berg","year":"1988","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrc.2008.05.019_bib44","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1111\/j.1365-2958.1996.tb02535.x","article-title":"Sequence specificity for DNA binding by Escherichia coli SoxS and Rob proteins","volume":"20","author":"Li","year":"1996","journal-title":"Mol. Microbiol."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X08008826?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X08008826?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T10:37:53Z","timestamp":1757759873000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X08008826"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2008,8]]},"references-count":44,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2008,8]]}},"alternative-id":["S0006291X08008826"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2008.05.019","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2008,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The iscS gene deficiency affects the expression of pyrimidine metabolism genes","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2008.05.019","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2008 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}