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Related Experiment Videos

E. coli RNAase P has a required RNA component.

R Kole, M F Baer, B C Stark

    Cell
    |April 1, 1980
    PubMed
    Summary
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    Mutations in the protein or RNA components of Ribonuclease P (RNAase P) can cause thermal sensitivity in E. coli. This study identifies specific component defects responsible for heat inactivation in mutant strains.

    Area of Science:

    • Molecular Biology
    • Enzymology
    • Microbial Genetics

    Background:

    • Ribonuclease P (RNAase P) is essential for bacterial tRNA maturation.
    • Thermosensitive mutations in E. coli can affect RNAase P function.
    • Understanding RNAase P thermal sensitivity provides insights into enzyme structure-function relationships.

    Purpose of the Study:

    • To investigate the molecular basis of thermal inactivation in thermosensitive RNAase P mutants of E. coli.
    • To determine whether protein or RNA components are responsible for thermal sensitivity.
    • To characterize the RNAase P enzyme from specific mutant strains and their revertants.

    Main Methods:

    • Partial purification of RNAase P from wild-type and three thermosensitive E. coli strains.
    • Determination of thermal inactivation characteristics of purified RNAase P preparations.

    Related Experiment Videos

  • Separation of RNAase P into RNA and protein components and in vitro reconstitution.
  • Analysis of RNA component quantity and protein component charge.

    • Main Results:

    • The protein component of RNAase P from ts241 and the RNA component from ts709 confer thermal sensitivity.
    • The ts709 mutant exhibits a lower amount of the RNA component compared to wild-type and ts241.
    • A revertant strain (A49) shows an altered charge in its RNAase P protein component.

    Conclusions:

    • Mutations affecting either the protein or RNA component of RNAase P can lead to thermal sensitivity.
    • Both in vivo and in vitro thermal sensitivity are conferred by these component mutations.
    • RNAase P thermal sensitivity is linked to defects in either its protein or RNA subunit.