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

The synthesis of heat-shock proteins after a decrease in translational capacity in Escherichia coli.

J Schnier1

  • 1Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann, Berlin, FRG.

Journal of General Microbiology
|November 1, 1987
PubMed
Summary

Decreased translational capacity and increased ribosomal synthesis in E. coli do not induce heat-shock proteins; instead, their synthesis is reduced. This finding challenges previous assumptions about stress responses in bacteria.

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

The cornerstone ceremony.

Psychoanalytic review·2010
Same author

Dragon lady.

The American imago; a psychoanalytic journal for the arts and sciences·2010
Same author

Congenital myasthenic syndrome caused by two non-N88K rapsyn mutations.

Clinical genetics·2007
Same author

Stimulation of protein synthesis in COS cells transfected with variants of the alpha-subunit of initiation factor eIF-2.

The Journal of biological chemistry·1992
Same author

Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.

Molecular and cellular biology·1991
Same author

Isolation and characterization of Bacillus stearothermophilus 30S and 50S ribosomal protein mutations.

Journal of bacteriology·1990

Area of Science:

  • Microbiology
  • Molecular Biology
  • Bacterial Stress Response

Background:

  • Heat-shock proteins (HSPs) are crucial for cellular protection under stress.
  • Bacterial translational capacity and ribosomal synthesis are tightly regulated.
  • The relationship between translational capacity, ribosome biogenesis, and HSP synthesis is not fully understood.

Purpose of the Study:

  • To investigate the effect of decreased translational capacity and enhanced ribosomal synthesis on heat-shock protein (HSP) production in Escherichia coli.
  • To determine if inhibiting ribosome formation or reducing translation induces stress proteins.

Main Methods:

  • Studied Escherichia coli under conditions that decrease translational capacity: streptomycin deprivation, tetracycline addition, and nutritional shift-up.

Related Experiment Videos

  • Monitored the synthesis rates of specific HSPs (DnaK, GroEL, C62.5) and ribosomal components.
  • Main Results:

    • In all tested conditions, the synthesis of HSPs DnaK, GroEL, and C62.5 decreased.
    • Concurrently, the synthesis of ribosomal components was observed to increase.
    • This indicates an inverse relationship between translational capacity reduction and HSP synthesis.

    Conclusions:

    • Inhibition of ribosome formation or a decrease in translational capacity does not induce heat-shock proteins in E. coli.
    • These conditions have the opposite effect, reducing the synthesis of key stress proteins.
    • Bacterial stress response mechanisms are more complex than previously assumed, with translational control playing a regulatory role.