doi: 10.1016/0300-9084(90)90187-l.
Protection from chemical modification of nucleotides in complexes of M1 RNA, the catalytic subunit of RNase P from E coli, and tRNA precursors
Affiliations
- PMID: 1707681
- DOI: 10.1016/0300-9084(90)90187-l
Item in Clipboard
Protection from chemical modification of nucleotides in complexes of M1 RNA, the catalytic subunit of RNase P from E coli, and tRNA precursors
Biochimie.
1990 Nov.
Free article
Abstract
Certain nucleotides in M1 RNA, the catalytic RNA subunit of RNase P from E coli, are protected from chemical modification when M1 RNA forms complexes with tRNA precursor molecules (ES complexes). Many of these nucleotides are important in the formation of the Michaelis complex. In the presence of tRNA precursor molecules, the pattern of protection from chemical modification of a region in M1 RNA that resembles the E site in 23S rRNA is similar to the pattern of protection of the E site in the presence of deacylated tRNA. In the complex with the RNA enzyme, more nucleotides in the substrate become accessible to modification, an indication that the substrate is in an unfolded conformation under these conditions.
Similar articles
-
Identification of a region within M1 RNA of Escherichia coli RNase P important for the location of the cleavage site on a wild-type tRNA precursor.J Mol Biol. 1993 Jun 5;231(3):594-604. doi: 10.1006/jmbi.1993.1312. J Mol Biol. 1993. PMID: 7685824
-
A physical assay for and kinetic analysis of the interactions between M1 RNA and tRNA precursor substrates.Biochemistry. 1993 Jul 20;32(28):7152-61. doi: 10.1021/bi00079a012. Biochemistry. 1993. PMID: 7688247
-
Artificial self-cleaving molecules consisting of a tRNA precursor and the catalytic RNA of RNase P.Nucleic Acids Res. 1993 Oct 11;21(20):4685-9. doi: 10.1093/nar/21.20.4685. Nucleic Acids Res. 1993. PMID: 8233817 Free PMC article.
-
RNase P from bacteria. Substrate recognition and function of the protein subunit.Mol Biol Rep. 1995-1996;22(2-3):99-109. doi: 10.1007/BF00988713. Mol Biol Rep. 1995. PMID: 8901495 Review.
-
Genetic analysis of the structure and function of RNase P from E. coli.Mol Biol Rep. 1995-1996;22(2-3):111-4. doi: 10.1007/BF00988714. Mol Biol Rep. 1995. PMID: 8901496 Review.
Cited by
-
Differential effects of the protein cofactor on the interactions between an RNase P ribozyme and its target mRNA substrate.Nucleic Acids Res. 2000 Aug 15;28(16):3105-16. doi: 10.1093/nar/28.16.3105. Nucleic Acids Res. 2000. PMID: 10931926 Free PMC article.
-
Interaction of the 3'-end of tRNA with ribonuclease P RNA.Nucleic Acids Res. 1994 Oct 11;22(20):4087-94. doi: 10.1093/nar/22.20.4087. Nucleic Acids Res. 1994. PMID: 7524035 Free PMC article.
-
UV cross-link mapping of the substrate-binding site of an RNase P ribozyme to a target mRNA sequence.RNA. 1999 Sep;5(9):1235-47. doi: 10.1017/s1355838299990672. RNA. 1999. PMID: 10496224 Free PMC article.
-
Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme.J Bacteriol. 1995 Apr;177(8):1919-28. doi: 10.1128/jb.177.8.1919-1928.1995. J Bacteriol. 1995. PMID: 7536728 Free PMC article. Review. No abstract available.
-
Reconstitution of enzymatic activity from fragments of M1 RNA.Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1266-70. doi: 10.1073/pnas.89.4.1266. Proc Natl Acad Sci U S A. 1992. PMID: 1741379 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
