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Literature summary for 3.1.26.11 extracted from
- Substitutions in conserved regions preceding and within the linker affect activity and flexibility of tRNase ZL, the long form of tRNase Z (2017), PLoS ONE, 12, e0186277 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in a baculovirus/insect Sf9 cell system | Drosophila melanogaster |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | Q8MKW7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Drosophila melanogaster |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the short form of tRNase Z, tRNase ZS, functions as a homodimer and is found in all prokaryotes and some eukaryotes. The long form, tRNase ZL, related to tRNase ZS through tandem duplication and found only in eukaryotes, possesses about 2000fold greater catalytic efficiency than tRNase ZS. tRNase ZL consists of related but diverged amino and carboxy domains connected by a flexible linker (also referred to as a flexible tether) and functions as a monomer. Biochemical exploration regions of Drosophila melanogaster tRNase Z through Ala scanning mutagenesis followed by processing kinetics is aided by analysis of flexibility using limited proteolysis and two-dimensional protein electrophoresis. This approach, informed by interpretation of a recent crystal structure of the Saccharomaces cerevisiae homolog, uncovers a hydrophobic subdomain formed across the amino domain-linker boundary, leading to the suggestion that peripheral substitutions affect the skeleton of twisted beta sheets in the amino domain on both sides of the flexible arm | Drosophila melanogaster |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | endonucleolytically removes 3' trailers from precursor tRNAs, preparing them for CCA addition and aminoacylation | Drosophila melanogaster |
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