Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Notes
Mutational Analysis of the Length of the J3/4 Domain of Escherichia coli Ribonuclease P Ribozyme
Shinnosuke HAGATerumichi TANAKAYo KIKUCHI
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2004 Volume 68 Issue 12 Pages 2630-2632

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Abstract

We prepared a series of length variants of the J3/4 domain of Escherichia coli ribonuclease P (RNase P) ribozyme: the four-base long J3/4 domain (A62G63G64A65) was replaced with GGA (denoted ΔA), GA (ΔAG), A (ΔAGG), AAGGA (ΣA), AAAGGA (ΣAA), and AAAAGGA (ΣAAA). The results indicated that truncating and inserting operations of the J3/4 domain drastically reduced ribozyme activity (WT>>ΣAA>ΣA>ΣAAA>>ΔAG>ΔA, ΔAGG), but did not affect the cleavage site selection of a substrate by the ribozyme. The reduced ribozyme activity of each mutant was rescued to some extent by the addition of a high concentration of magnesium ions. Our data indicate that the conserved AGGA sequence was important for efficient ribozyme reactions, and suggested that the length mutations affected ribozyme activity through metal ion binding steps.

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© 2004 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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