{"title":"CLONING OF A TWO-COMPONENT SIGNAL TRANSDUCTION SYSTEM OF XANTHOMONAS CAMPESTRIS PV. PHASEOLI VAR.FUSCANS STRAIN BXPF65","authors":"J. W. Chan, S. Maynard, P. Goodwin","doi":"10.1080/07060669809500395","DOIUrl":null,"url":null,"abstract":"A putative two-component signal transduction system was amplified and cloned from the plant pathogenic bacterium Xanthomonas campestris pv. phaseoli var. fuscans isolate BXPF65. The 620 bp amplified fragment was sequenced and analyzed with the BLAST Enhanced Alignment Utility (BEAUTY). BEAUTY analysis indicates that the putative xanthomonad response regulator contains regions which matched to an ATP phosphorylation site, a σ54-factor interaction domain, and the “receiver” domains of various transcriptional regulators of the two-component signal transduction systems. Similar analysis indicates that the putative histidine kinase has homology with conserved “transmitter” domains of sensor proteins in two-component signal transduction systems. RFLP analysis using the putative signal transduction system showed polymorphisms among the strains.","PeriodicalId":9607,"journal":{"name":"Canadian Journal of Plant Pathology-revue Canadienne De Phytopathologie","volume":"1120 1","pages":"288-295"},"PeriodicalIF":0.0000,"publicationDate":"1998-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Canadian Journal of Plant Pathology-revue Canadienne De Phytopathologie","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/07060669809500395","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
A putative two-component signal transduction system was amplified and cloned from the plant pathogenic bacterium Xanthomonas campestris pv. phaseoli var. fuscans isolate BXPF65. The 620 bp amplified fragment was sequenced and analyzed with the BLAST Enhanced Alignment Utility (BEAUTY). BEAUTY analysis indicates that the putative xanthomonad response regulator contains regions which matched to an ATP phosphorylation site, a σ54-factor interaction domain, and the “receiver” domains of various transcriptional regulators of the two-component signal transduction systems. Similar analysis indicates that the putative histidine kinase has homology with conserved “transmitter” domains of sensor proteins in two-component signal transduction systems. RFLP analysis using the putative signal transduction system showed polymorphisms among the strains.