Conserved motifs involved in ATP hydrolysis by MalT, a signal transduction ATPase with numerous domains from Escherichia coli.

ABSTRACT: The signal transduction ATPases with numerous domains (STAND) are sophisticated signaling proteins that are related to AAA+ proteins and control various biological processes, including apoptosis, gene expression, and innate immunity. They function as tightly regulated switches, with the off and on positions corresponding to an ADP-bound, monomeric form and an ATP-bound, multimeric form, respectively. Protein activation is triggered by inducer binding to the sensor domain. ATP hydrolysis by the nucleotide-binding oligomerization domain (NOD) ensures the generation of the ADP-bound form. Here, we use MalT, an Escherichia coli transcription activator, as a model system to identify STAND conserved motifs involved in ATP hydrolysis besides the catalytic acidic residue. Alanine substitution of t

SUBMITTER: Marquenet E 

PROVIDER: S-EPMC2944548 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature