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

Mapping structural differences between 30S ribosomal subunit assembly intermediates.

Kristi L Holmes1, Gloria M Culver

  • 1Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.

Nature Structural & Molecular Biology
|January 20, 2004
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

Evolution and adoption of contributor role ontologies and taxonomies.

Learned publishing : journal of the Association of Learned and Professional Society Publishers·2026
Same author

An exploratory survey about using ChatGPT in education, healthcare, and research.

PloS one·2023
Same author

A systematic scoping review of the ethics of Contributor Role Ontologies and Taxonomies.

Accountability in research·2023
Same author

Learn to fly: Training and competencies to support the multidisciplinary workforce needs of learning health systems.

Learning health systems·2022
Same author

Interdependency and Redundancy Add Complexity and Resilience to Biogenesis of Bacterial Ribosomes.

Annual review of microbiology·2022
Same author

Uncovering a delicate balance between endonuclease RNase III and ribosomal protein S15 in E. coli ribosome assembly.

Biochimie·2021

Functional Escherichia coli 30S ribosomal subunits assemble in vitro. A low-temperature intermediate (RI) transitions to RI* at higher temperatures, facilitating final assembly through protein-dependent rRNA changes.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Functional Escherichia coli 30S ribosomal subunits can be assembled in vitro from purified components.
  • Ribosome assembly is a complex process involving numerous protein and RNA interactions.
  • Low temperatures can stall the assembly process, leading to intermediate structures.

Purpose of the Study:

  • To investigate the structural and functional transition of an intermediate particle (RI) to a precursor particle (RI*) during 30S ribosomal subunit assembly.
  • To understand the role of ribosomal proteins (r-proteins) and ribosomal RNA (rRNA) in this transition.
  • To elucidate the molecular mechanisms underlying the formation of functional 30S subunits.

Main Methods:

  • In vitro assembly of Escherichia coli 30S ribosomal subunits.

Related Experiment Videos

  • Isolation and characterization of assembly intermediates (RI and RI*) by sedimentation analysis.
  • Chemical modification and primer extension analysis to probe 16S rRNA reactivity.
  • Integration of biochemical data with structural and biochemical information.

    • Main Results:

    • A stable intermediate (RI) forms at low temperatures, comprising 16S rRNA and a subset of r-proteins.
    • Incubation at elevated temperatures converts RI to RI* (26S particle) with similar composition but altered properties.
    • The transition from RI to RI* involves significant, r-protein-dependent changes in 16S rRNA reactivity, particularly in functional regions.
    • RI* rapidly associates with remaining r-proteins to form mature 30S subunits.

    Conclusions:

    • The transition from RI to RI* is a critical, protein-regulated step in the in vitro assembly of functional 30S ribosomal subunits.
    • Changes in rRNA structure and accessibility during this transition are crucial for subsequent assembly steps.
    • This study provides insights into the dynamic nature of ribosome assembly and the interplay between rRNA and r-proteins.