Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Specific interactions in RNA enzyme-substrate complexes.

C Guerrier-Takada1, N Lumelsky, S Altman

  • 1Department of Biology, Yale University, New Haven, CT 06520.

Science (New York, N.Y.)
|December 22, 1989
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

[Modified Oligonucleotides for Guiding RNA Cleavage Using Bacterial RNase P].

Molekuliarnaia biologiia·2019
Same author

Mesyl phosphoramidate antisense oligonucleotides as an alternative to phosphorothioates with improved biochemical and biological properties.

Proceedings of the National Academy of Sciences of the United States of America·2019
Same author

Antibiotics present and future.

FEBS letters·2013
Same author

The economic impact of anastomotic leakage after anterior resections in English NHS hospitals: are we adequately remunerating them?

Colorectal disease : the official journal of the Association of Coloproctology of Great Britain and Ireland·2013
Same author

Neuropsychological correlates of the PANSS Cognitive Factor.

Psychopathology·2004
Same author

Outcome measurement in pharmacological trials: validity of the Routine Assessment of Patient Progress (RAPP).

Journal of psychopharmacology (Oxford, England)·2004
Same journal

Erratum for the Research Article "Detecting supramolecular organic nanoparticles during heat wave".

Science (New York, N.Y.)·2026
Same journal

Local signals, systemic decline.

Science (New York, N.Y.)·2026
Same journal

The mechanics of liver regeneration.

Science (New York, N.Y.)·2026
Same journal

Computing in a memory with physics.

Science (New York, N.Y.)·2026
Same journal

Retraction.

Science (New York, N.Y.)·2026
Same journal

Making time.

Science (New York, N.Y.)·2026
See all related articles

Researchers studied M1 RNA, a catalytic RNA, and its interaction with transfer RNA precursors. Deleting a specific nucleotide (C92) in M1 RNA altered substrate cleavage sites, revealing key enzyme-substrate contact points.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • RNA catalysis

Background:

  • Ribonuclease P (RNase P) is a ribonucleoprotein enzyme responsible for tRNA maturation.
  • M1 RNA is the catalytic RNA component of bacterial RNase P.
  • Understanding enzyme-substrate interactions is crucial for elucidating catalytic mechanisms.

Purpose of the Study:

  • To investigate the structural and functional interactions between M1 RNA and its tRNA precursor substrates.
  • To identify specific nucleotides in M1 RNA involved in substrate binding and catalysis.
  • To determine how substrate features influence the site of RNA cleavage.

Main Methods:

  • Crosslinking analysis to map enzyme-substrate proximity.
  • Site-directed mutagenesis to delete specific M1 RNA residues (e.g., C92).

Related Experiment Videos

  • Analysis of cleavage activity of wild-type and mutant M1 RNA with various tRNA precursors.

    • Main Results:

    • Identified specific regions of M1 RNA and tRNA precursors in close physical contact.
    • Deletion of M1 RNA residue C92 resulted in altered cleavage sites, particularly for substrates lacking the 3' CCAUCA sequence.
    • The 3' terminal CCAUCA sequence significantly impacts substrate interaction with M1 RNA.
    • M1 RNA-substrate contacts share similarities with the tRNA 'E' (exit) site in 23S ribosomal RNA.

    Conclusions:

    • M1 RNA contains a nucleotide (C92) that influences the enzyme's cleavage site specificity.
    • Structural and functional domains can be conserved across RNA molecules with different cellular roles.
    • The interaction between M1 RNA and tRNA precursors is dynamic and influenced by substrate sequence, particularly the 3' terminus.