Identification of the Acinetobacter baumannii Ribonuclease P Catalytic Subunit: Cleavage of a Target mRNA in the Presence of an External Guide Sequence [PDF]
The bacterial ribonuclease P or RNase P holoenzyme is usually composed of a catalytic RNA subunit, M1, and a cofactor protein, C5. This enzyme was first identified for its role in maturation of tRNAs by endonucleolytic cleavage of the pre-tRNA. The RNase
Carol Davies-Sala+6 more
doaj +2 more sources
Eukaryotic Ribonuclease P: A Plurality of Ribonucleoprotein Enzymes [PDF]
▪ Abstract Ribonuclease P (RNase P) is an essential endonuclease that acts early in the tRNA biogenesis pathway. This enzyme catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5′ end of tRNAs. RNase P activities have been identified in Bacteria, Archaea, and Eucarya, as well as organelles.
Shaohua Xiao+3 more
openalex +4 more sources
Subsites for substrate recognition by bacterial ribonuclease P [PDF]
We have prepared series of shape variant RNAs of a tRNA precursor and analyzed the substrate shape recognition by bacterial ribonuclease P ribozyme and holoenzyme. The results showed the evidence for the presence of subsites for the recognition of the trna shape.
Atsuko Fujimoto+4 more
openalex +4 more sources
Bacterial RNA-free RNase P: Structural and functional characterization of multiple oligomeric forms of a minimal protein-only ribonuclease P. [PDF]
Wilhelm CA+10 more
europepmc +3 more sources
Modulation of ribonuclease P activity by calcipotriol [PDF]
The effects of cholesterol, 7‐dehydrocholesterol, vitamin D3 and several synthetic vitamin D3 analogs on ribonuclease P (RNase P) were investigated using a cell‐free system from the slime mold Dictyostelium discoideum. RNase P is an ubiquitous and essential enzyme that endonucleolytically cleaves all tRNA precursors to produce the mature 5′ end.
Evangelia Papadimou+4 more
openalex +4 more sources
Ribonuclease P: function and variation.
Norman R. Pace, Danielle Smith
openalex +4 more sources
Distributive enzyme binding controlled by local RNA context results in 3' to 5' directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P. [PDF]
Zhao J, Harris ME.
europepmc +2 more sources
Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA. [PDF]
Reiter NJ+5 more
europepmc +3 more sources
Production of ovine Pancreatic Ribonuclease and investigation of enzyme characteristics [PDF]
Introduction Obviously, the recent decades strategy in cancer therapy, anticancer drug discovery and drug improvement is to characterize, distinguish and validate the most promising cancer-related molecular targets to which new drugs can be designed. The
mahsa Zabetian+3 more
doaj +1 more source
Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P
RNA-based enzyme RNase P is a ribonucleoprotein complex responsible primarily for 5’-maturation of tRNAs. S. cerevisiae RNase P comprises a catalytic RNA component and nine proteins. The assembly and maturation of S.
Anna Perederina+2 more
doaj +1 more source