PMID:23344958
| Citation |
Lu, F and Taghbalout, A (2013) Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II. J. Biol. Chem. 288:7241-51 |
|---|---|
| Abstract |
The subcellular localization of the exoribonuclease RNase II is not known despite the advanced biochemical characterization of the enzyme. Here we report that RNase II is organized into cellular structures that appear to coil around the Escherichia coli cell periphery and that RNase II is associated with the cytoplasmic membrane by its amino-terminal amphipathic helix. The helix also acts as an autonomous transplantable membrane binding domain capable of directing normally cytoplasmic proteins to the membrane. Assembly of the organized cellular structures of RNase II required the RNase II amphipathic membrane binding domain. Co-immunoprecipitation of the protein from cell extracts indicated that RNase II interacts with itself. The RNase II self-interaction and the ability of the protein to assemble into organized cellular structures required the membrane binding domain. The ability of RNase II to maintain cell viability in the absence of the exoribonuclease polynucleotide phosphorylase was markedly diminished when the RNase II cellular structures were lost due to changes in the amphipathicity of the amino-terminal helix, suggesting that membrane association and assembly of RNase II into organized cellular structures play an important role in the normal function of the protein within the bacterial cell. |
| Links |
PubMed PMC3591632 Online version:10.1074/jbc.M112.408674 |
| Keywords |
Amino Acid Sequence; Binding Sites/genetics; Blotting, Western; Cell Membrane/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Exoribonucleases/chemistry; Exoribonucleases/genetics; Exoribonucleases/metabolism; Hydrophobic and Hydrophilic Interactions; Luminescent Proteins/genetics; Luminescent Proteins/metabolism; Microbial Viability; Microscopy, Fluorescence; Models, Molecular; Mutation; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary |
| 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.