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PMID:16301313

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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

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:LDCI

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P31473

F

Seeded From UniProt

complete

ECOLI:VIAA

acts_upstream_of_or_within

GO:0032781: positive regulation of ATP-dependent activity

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:RAVA

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P31473

F

Seeded From UniProt

complete

ECOLI:RAVA

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A9H3

F

Seeded From UniProt

complete

ECOLI:RAVA

located_in

GO:0005737: cytoplasm

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

ECOLI:RAVA

enables

GO:0016887: ATP hydrolysis activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ECOLI:LDCI

enables

GO:0008923: lysine decarboxylase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ECOLI:LDCI

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A9H3

F

Seeded From UniProt

complete

See also

References

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