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• W334843571 abstract "Research Article1 April 1991free access A single-stranded DNA binding protein from S. cerevisiae specifically recognizes the T-rich strand of the core sequence of ARS elements and discriminates against mutant sequences. A. M. Schmidt A. M. Schmidt Laboratorium für Biochemie, Universität Bayreuth, Germany. Search for more papers by this author S. U. Herterich S. U. Herterich Laboratorium für Biochemie, Universität Bayreuth, Germany. Search for more papers by this author G. Krauss G. Krauss Laboratorium für Biochemie, Universität Bayreuth, Germany. Search for more papers by this author A. M. Schmidt A. M. Schmidt Laboratorium für Biochemie, Universität Bayreuth, Germany. Search for more papers by this author S. U. Herterich S. U. Herterich Laboratorium für Biochemie, Universität Bayreuth, Germany. Search for more papers by this author G. Krauss G. Krauss Laboratorium für Biochemie, Universität Bayreuth, Germany. Search for more papers by this author Author Information A. M. Schmidt1, S. U. Herterich1 and G. Krauss1 1Laboratorium für Biochemie, Universität Bayreuth, Germany. The EMBO Journal (1991)10:981-985https://doi.org/10.1002/j.1460-2075.1991.tb08032.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info A protein named ssARS-T binding protein has been purified from yeast that specifically binds to the T-rich strand of the consensus core sequence of yeast autonomously replicating sequence (ARS) elements. As assayed from gel mobility shift experiments the ssARS-T protein shows characteristics of a sequence specific single-stranded DNA binding protein. The complementary A-rich strand of the ARS core sequence is bound much more weakly and no binding can be detected for the double-stranded form of the core sequence. Three single base substitutions in the core sequence that are known to abolish ARS function in vivo also lead to weaker binding of the core sequence to the ssARS-T protein in vitro. The strong correlation between the binding of mutated sequences in vitro and the ARS properties of these sequences in vivo points to an essential function of the ssARS-T protein during replication initiation in yeast ARS elements. Previous ArticleNext Article Volume 10Issue 41 April 1991In this issue RelatedDetailsLoading ..." @default.
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• W334843571 title "A single-stranded DNA binding protein from S. cerevisiae specifically recognizes the T-rich strand of the core sequence of ARS elements and discriminates against mutant sequences." @default.
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• W334843571 doi "https://doi.org/10.1002/j.1460-2075.1991.tb08032.x" @default.
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