PMID:7694652
| Citation |
Hardt, WD, Schlegl, J, Erdmann, VA and Hartmann, RK (1993) Role of the D arm and the anticodon arm in tRNA recognition by eubacterial and eukaryotic RNase P enzymes. Biochemistry 32:13046-53 |
|---|---|
| Abstract |
Truncated precursor tRNAs lacking the D arm or anticodon arm were studied in vitro as substrates for RNase P enzymes from Escherichia coli, Thermus thermophilus (eubacteria), and HeLa. Deletion of the D arm still allowed 5'-processing by E. coli RNase P, but strongly impaired maturation by T. thermophilus and HeLa extracts. In contrast, deletion of the anticodon arm had no influence on processing by RNase P activities from all three organisms. Inhibition kinetics and gel retardation studies showed that deletion of the D arm leads to low-affinity binding to E. coli RNase P RNA (M1 RNA). However, the E. coli enzyme appears to form sufficiently strong contacts in the region of the T arm, acceptor stem, and CCA terminus to still allow productive enzyme-substrate interaction even in the absence of the structural contribution provided by the D arm. Pb(2+)-induced hydrolysis of a tRNAGly from T. thermophilus gave identical cleavage patterns in the D arm and anticodon loop in the absence and presence of E. coli M1 RNA, whereas lead hydrolysis was strongly reduced at the CUCCAA 3'-terminus due to the presence of the enzyme. |
| Links | |
| Keywords |
Anticodon/metabolism; Base Sequence; Binding Sites; Cations, Monovalent; Endoribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; HeLa Cells; Humans; Hydrogen Bonding; Lead/chemistry; Molecular Sequence Data; Nucleic Acid Conformation; Nucleic Acid Precursors/metabolism; RNA Processing, Post-Transcriptional; RNA, Bacterial/metabolism; RNA, Catalytic/metabolism; RNA, Transfer, Gly/chemistry; RNA, Transfer, Gly/metabolism; Ribonuclease P; Sequence Deletion; Structure-Activity Relationship; Substrate Specificity; Thermus thermophilus/enzymology |
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