PMID:11258957
| Citation |
Zuleeg, T, Hansen, A, Pfeiffer, T, Schübel, H, Kreutzer, R, Hartmann, RK and Limmer, S (2001) Correlation between processing efficiency for ribonuclease P minimal substrates and conformation of the nucleotide -1 at the cleavage position. Biochemistry 40:3363-9 |
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| Abstract |
It is demonstrated that acceptor stem duplexes derived from native tRNAs which contain a three-nucleotide extension at the 5'-terminus of mature tRNA are minimal substrates for ribonuclease P from both Escherichia coli and Bacillus subtilis. Variants with a cytidine at position -1 are most efficiently processed whereas the G -1 variant represents a comparatively poor substrate. An A -1 acceptor stem variant is a slightly better substrate than the G -1 variant though generally distinctly less efficient than the C -1 duplex. This is in qualitative agreement with the frequency of the occurrence of the corresponding nucleotides at position -1 in natural substrates, which is highest for pyrimidines and least for G. NMR analyses of the corresponding acceptor stems reveal that the conformation of the nucleotides at position -1 correlates with the substrate preferences of Ribonuclease P: Whereas C -1 adopts a conformation characterized by a glycosidic angle in the anti range (close to high-anti), the G -1 is clearly in syn conformation, and that of A -1 is intermediate between high-anti and syn. The riboses of nucleotides -1 are in all cases predominantly 2'-endo puckered. |
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| Keywords |
Adenosine/metabolism; Bacillus subtilis/enzymology; Base Composition; Cytidine/metabolism; Endoribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Guanosine/metabolism; Hydrolysis; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Nucleic Acid Conformation; Nucleic Acid Heteroduplexes/metabolism; RNA Processing, Post-Transcriptional; RNA, Catalytic/metabolism; RNA, Transfer/metabolism; Ribonuclease P; Substrate Specificity |
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