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| Domain structure of the ribozyme from eubacterial ribonuclease P |
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| Author(s): Loria A, Pan T |
| Source: RNA-A PUBLICATION OF THE RNA SOCIETY Volume: 2 Issue: 6 Pages: 551-563 Published: JUN 1996 |
| Times Cited: 107 References: 26 |
| Abstract: Large RNAs can be composed of discrete domains that fold independently. One such ''folding domain'' has been identified previously in the ribozyme from Bacillus subtilis ribonuclease P (denoted P RNA). This domain contains roughly one-third of all residues, Folding of an RNA construct consisting of the remaining two-thirds of B. subtilis P RNA was examined by Fe(II)-EDTA hydroxyl radical protection. This molecule folds into the proper higher-order structure under identical conditions as the full-length P RNA, suggesting the presence of a second folding domain in B. subtilis P RNA. Folding analysis of the Escherichia coli P RNA by hydroxyl radical protection shows that this P RNA is completely folded at 5-6 mM Mg2+. I, order to analyze the structural organization of folding domains in E. coli P RNA, constructs were designed based on the domain structure of B. subtilis P RNA. Fe(II)-EDTA protection indicates that E. coli P RNA also contains two folding domains. Despite the significant differences at the secondary structure level, both P RNAs appear to converge structurally at the folding domain level. The pre-tRNA substrate, localized in previous studies, may bind across the folding domains with the acceptor stem/3'CCA contacting the domain including the active site and the T stem-loop contacting the other. Because all eubacterial P RNAs share considerable homology in secondary structure to either B. subtilis or E. coli P RNA, these results suggest that this domain structure may be applicable for most, if not all, eubacterial P RNAs. Identification of folding domains should be valuable in dissecting structure-function relationship of large RNAs. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV CHICAGO, DEPT BIOCHEM & MOLEC BIOL, CHICAGO, IL 60637 USA |
| Publisher: CAMBRIDGE UNIV PRESS, 40 WEST 20TH STREET, NEW YORK, NY 10011-4211 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: UY700 |
| ISSN: 1355-8382 |
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