Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | RNase II is organized into cellular structures that appear to coil around the Escherichia coli cell periphery. The ability of RNase II to maintain cell viability in the absence of exoribonuclease polynucleotide phosphorylase is markedly diminished when the RNase II cellular structures are lost due to changes in the amphipathicity of the amino-terminal helix | Escherichia coli | 9986 | - |
membrane | 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 | Escherichia coli | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P30850 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
RNase II | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | RNase II self-interaction and the ability of the protein to assemble into organized cellular structures requires the membrane binding domain. The ability of RNase II to maintain cell viability in the absence of exoribonuclease polynucleotide phosphorylase is markedly diminished when the RNase II cellular structures are lost due to changes in the amphipathicity of the amino-terminal helix | Escherichia coli |