MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator.
AUTOR(ES)
Richet, E
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=400900Documentos Relacionados
- Expression of malT, the regulator gene of the maltose region in Escherichia coli, is limited both at transcription and translation.
- The N Terminus of the Escherichia coli Transcription Activator MalT Is the Domain of Interaction with MalY
- Characterization of malT mutants that constitutively activate the maltose regulon of Escherichia coli.
- ATP-dependent renaturation of DNA catalyzed by the recA protein of Escherichia coli.
- Transfer RNA is an essential component of the ubiquitin- and ATP-dependent proteolytic system.