Bacterial ribonuclease P reaction is affected by substrate shape and magnesium ion concentration
نویسندگان
چکیده
منابع مشابه
The protein component of bacterial ribonuclease P flickers the metal ion response to the substrate shape preference of the ribozyme.
The substrate shape specificity of the Escherichia coli ribonuclease P (RNase P) ribozyme depends on the concentration of magnesium ion. At 10 mM or more, it can cleave a hairpin substrate as well as a cloverleaf pre-transfer RNA (tRNA). The results showed, however, that the holo enzyme cleaved the hairpin substrate at low concentrations of magnesium ion. Considering that the homologous E. coli...
متن کاملDependence of M1 RNA substrate specificity on magnesium ion concentration.
We have constructed a plasmid expressing E. coli M1 RNA, the catalytic RNA subunit of ribonuclease P, under the control of a phage T7 promoter. The active M1 RNA species synthesized in vitro by T7 RNA polymerase from this vector was reacted with the tRNA(Gln) - tRNA(Leu) precursor RNA (Band K) encoded by phage T4. Only the tRNA(Leu) moiety of this dimeric precursor RNA contains the 3' terminal ...
متن کاملComparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes.
Previously, we reported that the substrate shape recognition of the Escherichia coli ribonuclease (RNase) P ribozyme depends on the concentration of magnesium ion in vitro. We additionally examined the Bacillus subtilis RNase P ribozyme and found that the B. subtilis enzyme also required high magnesium ion, above 10 mM, for cleavage of a hairpin substrate. The results of kinetic studies showed ...
متن کاملThe bacterial ribonuclease P holoenzyme requires specific, conserved residues for efficient catalysis and substrate positioning
RNase P is an RNA-based enzyme primarily responsible for 5'-end pre-tRNA processing. A structure of the bacterial RNase P holoenzyme in complex with tRNAPhe revealed the structural basis for substrate recognition, identified the active site location, and showed how the protein component increases functionality. The active site includes at least two metal ions, a universal uridine (U52), and P R...
متن کاملComparative Analyses of Hairpin and BaciUus subtMs RibonucleaseSubstrate Recognition P Ribozym s JSen by Escherichia coli
Previously, we reported that the substrate shape recognition of the EScherichia coli ribonuclease (RNase) P ribozyme depends on the eoncentration of magnesium ion in vitro. We additional]y examined the Bacillvs subtilts RNase P ribozyme and found that the B. subti1ts enzyme also required high mag"esium ion, aboye 10 mM, for cleavage of a hairpin substrate. The results of kinetic studies showed ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nucleic Acids Symposium Series
سال: 2003
ISSN: 0261-3166,1746-8272
DOI: 10.1093/nass/3.1.293