PMID:21527254
| Citation |
Tomar, SK, Kumar, P and Prakash, B (2011) Deciphering the catalytic machinery in a universally conserved ribosome binding ATPase YchF. Biochem. Biophys. Res. Commun. 408:459-64 |
|---|---|
| Abstract |
YchF, a universally conserved protein, hitherto thought to be a GTPase, was shown to be an ATPase based on structural and biochemical studies on hOLA1, a human ortholog of YchF. However, the cellular role of YchF is unclear. Based on the presence of a RNA binding domain in this protein and significant homology to ribosome binding Obg family GTPases, we examined its ability to associate with the ribosome. Here, we show that Escherichia coli YchF binds the 50S and 70S ribosomal particles in a nucleotide independent manner and it hydrolyzes ATP utilizing a potassium dependent mechanism. A potassium mediated acceleration of hydrolysis activity was thus far known for a few GTPases. Like these, YchF too conserves the structural features required for K(+) coordination, making it a unique ribosome binding ATPase utilizing a similar mechanism. Furthermore, we show that Lys78 is an important determinant of the potassium dependent ATPase activity. |
| Links |
PubMed Online version:10.1016/j.bbrc.2011.04.052 |
| Keywords |
Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Catalysis; Conserved Sequence; Escherichia coli/enzymology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Molecular Sequence Data; Potassium/metabolism; Ribosomes/metabolism |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
See also
References
See Help:References for how to manage references in EcoliWiki.