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MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator.

1989; Springer Nature; Volume: 8; Issue: 3 Linguagem: Inglês

10.1002/j.1460-2075.1989.tb03461.x

1460-2075

Evelyne Richet, Olivier Raibaud,

RNA and protein synthesis mechanisms

Research Article1 March 1989free access MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator. E. Richet E. Richet Unité de Génétique Moléculaire, Institut Pasteur, Paris, France. Search for more papers by this author O. Raibaud O. Raibaud Unité de Génétique Moléculaire, Institut Pasteur, Paris, France. Search for more papers by this author E. Richet E. Richet Unité de Génétique Moléculaire, Institut Pasteur, Paris, France. Search for more papers by this author O. Raibaud O. Raibaud Unité de Génétique Moléculaire, Institut Pasteur, Paris, France. Search for more papers by this author Author Information E. Richet1 and O. Raibaud1 1Unité de Génétique Moléculaire, Institut Pasteur, Paris, France. The EMBO Journal (1989)8:981-987https://doi.org/10.1002/j.1460-2075.1989.tb03461.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We show that MalT, the transcriptional activator of the Escherichia coli maltose regulon, specifically binds ATP and dATP with a high affinity (Kd = 0.4 microM) and exhibits a weak ATPase activity. Using an abortive initiation assay, we further show that activation of open complex formation by MalT depends on the presence of ATP in addition to that of maltotriose, the inducer of the maltose system. Similar experiments in which ATP was replaced by ADP or AMP-PNP, a non-hydrolysable analogue of ATP, demonstrate that this reaction does not require ATP hydrolysis. As revealed by DNase I footprinting, both ATP and maltotriose are required for the binding of the MalT protein to the mal promoter DNA. Previous ArticleNext Article Volume 8Issue 31 March 1989In this issue RelatedDetailsLoading ...