Cloned (Comment) | Organism |
---|---|
expression of His-tagged subunits Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, and hPop5 in Escherichia coli | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
nucleus | - |
Homo sapiens | 5634 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged subunits Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, and hPop5 from Escherichia coli as soluble and refolded proteins | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
RNase P | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | the catalytic RNP has an H1 RNA moiety associated with ten distinct protein subunits. Five out of eight of these protein subunits, Rpp20, Rpp21, Rpp25, Rpp29, and Pop5, prepared in refolded recombinant forms, bind to H1 RNA in vitro. Rpp20 and Rpp25 bind jointly to H1 RNA, even though each protein can interact independently with this transcript. Nuclease footprinting analysis reveals that Rpp20 and Rpp25 recognize overlapping regions in the P2 and P3 domains of H1 RNA. Rpp21 and Rpp29, which are sufficient for reconstitution of the endonucleolytic activity, bind to separate regions in the catalytic domain of H1 RNA, subunit binding site analysis on H1 RNA, overview | Homo sapiens |
physiological function | nuclear RNase P is required for transcription and processing of tRNA | Homo sapiens |