ArticleProceedings of the National Academy of Sciences of the United States of America2001
A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator family.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 33 citations in OpenAlex.
- Structural basis for negative regulation of the Escherichia coli maltose system.Nature communications · 2023Article
- Prokaryotic innate immunity through pattern recognition of conserved viral proteins.Science (New York, N.Y.) · 2022Article
- The Application of Regulatory Cascades inFrontiers in microbiology · 2020Review
- Double autoinhibition mechanism of signal transduction ATPases with numerous domains (STAND) with a tetratricopeptide repeat sensor.Nucleic acids research · 2019Article
- Activation of microbial secondary metabolic pathways: Avenues and challenges.Synthetic and systems biotechnology · 2018Review
- Article
- Gene mdpC plays a regulatory role in the methyl-tert-butyl ether degradation pathway of Methylibium petroleiphilum strain PM1.FEMS microbiology letters · 2015Article
- The α-glucan phosphorylase MalP of Corynebacterium glutamicum is subject to transcriptional regulation and competitive inhibition by ADP-glucose.Journal of bacteriology · 2015Article
- How 'arm-twisting' by the inducer triggers activation of the MalT transcription factor, a typical signal transduction ATPase with numerous domains (STAND).Nucleic acids research · 2015Article
- Mycobacterium tuberculosis protein kinase K enables growth adaptation through translation control.Journal of bacteriology · 2012Article
- Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis.Nature biotechnology · 2006Article
- Parallel changes in global protein profiles during long-term experimental evolution in Escherichia coli.Genetics · 2006Article
- Identification of PimR as a positive regulator of pimaricin biosynthesis in Streptomyces natalensis.Journal of bacteriology · 2004Article
- The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY.Journal of bacteriology · 2002Article
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1 author at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
MalT, the specific activator of the maltose regulon, is the prototype of a family of high-molecular-mass ATP-binding bacterial transcription activators. On binding of its two positive effectors, the inducer maltotriose and ATP, MalT oligomerizes to an active state competent for promoter binding and transcription activation. In addition to its previously known DNA-binding domain, limited proteolysis showed that MalT contains three other domains, the boundaries of which were accurately delimited by N-terminal microsequencing. The N-terminal domain alone binds ATP. Maltotriose binding involves an extended region corresponding to domains 2 and 3, although weak binding to domain 3 alone was also observed. Moreover, maltotriose binding induces a conformational shift involving a movement of both domains 1 and 3 with respect to domain 2, leading to the active form of the protein. Sequence examination of the MalT homologues suggests that these three domains might constitute a signaling module.
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