Long-range structure in ribonuclease P RNA

doi:10.1126/science.1719634

Account Information

Guest Alerts | Access Rights | My Account | Sign In

Site Navigation

Article Views

Article Tools

My Science

Science 8 November 1991:
Vol. 254. no. 5033, pp. 853 - 856
DOI: 10.1126/science.1719634

Prev | Table of Contents | Next

Articles

Science, Vol 254, Issue 5033, 853-856
Copyright © 1991 by American Association for the Advancement of Science

articles

Long-range structure in ribonuclease P RNA

ES Haas, DP Morse, JW Brown, FJ Schmidt, and NR Pace

Department of Biology, Indiana University, Bloomington 47405.

Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA. This feature strongly constrains the three-dimensional structure of RNase P RNA near the active site. Some RNase P RNAs lack this structure but contain a unique, possibly compensating, structural domain. This suggests that different RNA structures located at different positions in the sequence may have equivalent architectural functions in RNase P RNA.

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:

Compensatory Evolution in RNA Secondary Structures Increases Substitution Rate Variation among Sites.: J. L. Knies, K. K. Dang, T. J. Vision, N. G. Hoffman, R. Swanstrom, and C. L. Burch (2008)
Mol. Biol. Evol. 25, 1778-1787
| Abstract » | Full Text » | PDF »

Folding of noncoding RNAs during transcription facilitated by pausing-induced nonnative structures.: T. N. Wong, T. R. Sosnick, and T. Pan (2007)
PNAS 104, 17995-18000
| Abstract » | Full Text » | PDF »

Deciphering RNA structural diversity and systematic phylogeny from microbial metagenomes.: Y. Zhu, D. K. Pulukkunat, and Y. Li (2007)
Nucleic Acids Res. 35, 2283-2294
| Abstract » | Full Text » | PDF »

Topological rearrangement yields structural stabilization and interhelical distance constraints in the Kin.46 self-phosphorylating ribozyme.: B. Cho and D. H. Burke (2006)
RNA 12, 2118-2125
| Abstract » | Full Text » | PDF »

Pleiotropic Effect of Disrupting a Conserved Sequence Involved in a Long-Range Compensatory Interaction in the Drosophila Adh Gene.: J. F. Baines, J. Parsch, and W. Stephan (2004)
Genetics 166, 237-242
| Abstract » | Full Text » | PDF »

Inhibition of Escherichia coli RNase P by oligonucleotide directed misfolding of RNA.: J. L. CHILDS, A. W. POOLE, and D. H. TURNER (2003)
RNA 9, 1437-1445
| Abstract » | Full Text » | PDF »

Bacterial ribonuclease P holoenzyme crosslinking analysis reveals protein interaction sites on the RNA subunit.: S. M. Sharkady and J. M. Nolan (2001)
Nucleic Acids Res. 29, 3848-3856
| Abstract » | Full Text » | PDF »

Comparative Sequence Analysis and Patterns of Covariation in RNA Secondary Structures.: J. Parsch, J. M. Braverman, and W. Stephan (2000)
Genetics 154, 909-921
| Abstract » | Full Text »

Cloning and Characterization of Three New Murine Genes Encoding Short Homologues of RNase P RNA.: K. Li and R. S. Williams (1995)
J. Biol. Chem. 270, 25281-25285
| Abstract » | Full Text » | PDF »

Yeast site-specific ribonucleoprotein endoribonuclease MRP contains an RNA component homologous to mammalian RNase MRP RNA and essential for cell viability..: M E Schmitt and D A Clayton (1992)
Genes & Dev. 6, 1975-1985
| Abstract » | PDF »