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© Research
Publication : Proceedings of the National Academy of Sciences of the United States of America

A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator family

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 16 Jan 2001

Danot O

Link to Pubmed [PMID] – 11209048

Proc. Natl. Acad. Sci. U.S.A. 2001 Jan;98(2):435-40

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.

http://www.ncbi.nlm.nih.gov/pubmed/11209048