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Journal ArticleDOI

Specific interaction between the self-splicing RNA of Tetrahymena and its guanosine substrate: implications for biological catalysis by RNA

Brenda L. Bass, +1 more
- 01 Jan 1984 - 
- Vol. 308, Iss: 5962, pp 820-826
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TLDR
Splicing of the ribosomal RNA precursor of Tetrahymena has previously been shown to require no protein in vitro; the cleavage–ligation activity is intrinsic to the RNA molecule, and analysis of the reaction kinetics suggests that guanosine binds to a specific site on the pre-rRNA.
Abstract
Splicing of the ribosomal RNA precursor of Tetrahymena has previously been shown to require no protein in vitro; the cleavage-ligation activity is intrinsic to the RNA molecule. Analysis of the reaction kinetics with guanosine, which is a substrate in the reaction, and with several guanosine analogues suggests that guanosine binds to a specific site on the pre-rRNA. It appears that the RNA, like an enzyme, binds its substrate to promote the rate and specificity of a biological reaction.

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Citations
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Journal ArticleDOI

The noncoding RNA revolution-trashing old rules to forge new ones.

TL;DR: The pathway of ncRNA research is described, where every established "rule" seems destined to be overturned.
Journal ArticleDOI

Why nature chose phosphates

TL;DR: Stable, negatively charged phosphates react under catalysis by enzymes; organic chemists, who can only rarely use enzymatic catalysis for their reactions, need more highly reactive intermediates than phosphates.
Patent

Rna ribozyme polymerases, dephosphorylases, restriction endoribonucleases and methods.

TL;DR: In this paper, a shortened form of the self-splicing ribosomal RNA intervening sequence of Tetrahymena (L-19 IVS RNA) is used to synthesize a set of sequence-specific endoribonucleases.
Journal ArticleDOI

The structural and functional diversity of metabolite-binding riboswitches.

TL;DR: A diverse set of metabolite-sensing RNAs is found to exploit a variety of distinct mechanisms to regulate genes that are fundamental to metabolism.
Journal ArticleDOI

The intervening sequence RNA of Tetrahymena is an enzyme.

TL;DR: The shortened form of the self-splicing ribosomal RNA intervening sequence of Tetrahymena thermophila acts as an enzyme in vitro that can act as an RNA polymerase, differing from the protein enzyme in that it uses an internal rather than an external template.
References
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Journal ArticleDOI

The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme

TL;DR: The RNA moieties of ribonuclease P purified from both E. coli and B. subtilis can cleave tRNA precursor molecules in buffers containing either 60 mM Mg2+ or 10 mM MG2+ plus 1 mM spermidine, and in vitro, the RNA and protein subunits from one species can complement sub units from the other species in reconstitution experiments.
Journal ArticleDOI

Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of tetrahymena

TL;DR: It is proposed that the IVS portion of the RNA has several enzyme-like properties that enable it to break and reform phosphodiester bonds and that enzymes, small nuclear RNAs and folding of the pre-rRNA into an RNP are unnecessary for these reactions.
Journal ArticleDOI

In vitro splicing of the ribosomal RNA precursor of tetrahymena: Involvement of a guanosine nucleotide in the excision of the intervening sequence

TL;DR: It is proposed that Tetrahymena pre-rRNA splicing occurs by a phosphoester transferase mechanism where the guanosine cofactor provides the free 3' hydroxyl necessary to initiate a series of three transfers that results in splicing of the pre- rRNA and cyclization of the excised IVS.
Journal ArticleDOI

Secondary structure of 16S ribosomal RNA

Harry F. Noller, +1 more
- 24 Apr 1981 - 
TL;DR: A secondary structure model for 16S ribosomal RNA which is based on available chemical, enzymatic, and comparative sequence data shows good agreement between constraints dictated by the model and a wide variety of experimental observations.
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