PMID:16301313
| Citation |
Snider, J, Gutsche, I, Lin, M, Baby, S, Cox, B, Butland, G, Greenblatt, J, Emili, A and Houry, WA (2006) Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase. J. Biol. Chem. 281:1532-46 |
|---|---|
| Abstract |
AAA+ ATPases are ubiquitous proteins that employ the energy obtained from ATP hydrolysis to remodel proteins, DNA, or RNA. The MoxR family of AAA+ proteins is widespread throughout bacteria and archaea but is largely uncharacterized. Limited work with specific members has suggested a potential role as molecular chaperones involved in the assembly of protein complexes. As part of an effort aimed at determining the function of novel AAA+ chaperones in Escherichia coli, we report the characterization of a representative member of the MoxR family, YieN, which we have renamed RavA (regulatory ATPase variant A). We show that the ravA gene exists on an operon with another gene encoding a protein, YieM, of unknown function containing a Von Willebrand Factor Type A domain. RavA expression is under the control of the sigmaS transcription factor, and its levels increase toward late log/early stationary phase, consistent with its possible role as a general stress-response protein. RavA functions as an ATPase and forms hexameric oligomers. Importantly, we demonstrate that RavA interacts strongly with inducible lysine decarboxylase (LdcI or CadA) forming a large cage-like structure consisting of two LdcI decamers linked by a maximum of five RavA oligomers. Surprisingly, the activity of LdcI does not appear to be affected by binding to RavA in a number of in vitro and in vivo assays, however, complex formation results in the stimulation of RavA ATPase activity. Data obtained suggest that the RavA-LdcI interaction may be important for the regulation of RavA activity against its targets. |
| Links |
PubMed Online version:10.1074/jbc.M511172200 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Carboxy-Lyases/classification; Carboxy-Lyases/isolation & purification; Carboxy-Lyases/metabolism; Chromatography, Gel; Conserved Sequence; Enzyme Induction; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/classification; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/metabolism; Molecular Sequence Data; Phylogeny |
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