Substrate Recognition Ability Differs Among Various Prokaryotic Trnase Zs.
From: Department of Applied Life Sciences, Niigata University of Pharmacy and Applied Life Sciences, Niigata, Niigata 956-8603, Japan.
Biochemical and biophysical research communications
- Publish Date: Jun 2006
- ISSN: 0006-291X
- Volume: 345
- Issue: 1
- Pages: 385-93
- Medium: Print
- Language: English
- Citation (JAMA): Minagawa Asako, Takaku Hiroaki, Shibata Hirotaka S, et al. Substrate Recognition Ability Differs Among Various Prokaryotic Trnase Zs.. Biochem. Biophys. Res. Commun. Jun 2006;345:385-93
Abstract
There exists a significant difference in pre-tRNA preference among prokaryotic tRNase Zs. This is an enigma, because pre-tRNAs should form the common L-shaped structure and tRNase Zs should form the common structure based on the alphabeta/betaalpha-fold. To address this issue, we examined six different eubacterial and archaeal tRNase Zs including two newly isolated tRNase Zs for cleavage of 18 different pre-tRNA substrates. Two Thermotoga maritima, one Thermus thermophilus, one Bacillus subtilis, one Thermoplasma acidophilum, and one Pyrobaculum aerophilum enzymes were tested. To our surprise, the newly isolated proteins T. maritima and T. thermophilus showed the weak tRNase Z activity, even though their primary amino acid sequences are, on the whole, quite different from those of the typical tRNase Zs. We confirmed that substrate recognition ability is quite different among those tRNase Zs. In addition, we found that the optimal conditions as a whole differ significantly among the enzymes. From these results, we provided several clues to solve the enigma by showing the potential importance of the 74th-76th nucleotide sequence of pre-tRNA, the flexible arm length of tRNase Z, the divalent metal ion species, and the histidine corresponding His222 in T. maritima tRNase Z.
Mesh Headings (Keywords): Amino Acid Sequence, Bacteria, Binding Sites, Drosophila Proteins, Endoribonucleases, Enzyme Activation, Enzyme Stability, Hydrogen-Ion Concentration, Molecular Sequence Data, Protein Binding, Species Specificity, Substrate Specificity, Temperature
Check for Full Text / PubMed Unique Identifier (PMID): 16681995
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