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 small-subunit processome is a ribosome assembly intermediate.

Kara A Bernstein1, Jennifer E G Gallagher, Brianna M Mitchell

  • 1Department of Molecular Biophysics and Biochemistry, Yale School of Medicine, C114 SHM, 333 Cedar St., New Haven, CT 06520-8024, USA.

Eukaryotic Cell
|December 14, 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

Saturation Genome Editing reveals the functional impact of RAD51D <i>and</i> XRCC2 variants.

bioRxiv : the preprint server for biology·2026
Same author

Structural insight into how RAD51 paralog exchange regulates RAD51 filament formation.

Nature structural & molecular biology·2026
Same author

Specifications of the ACMG/AMP variant curation guidelines for the analysis of germline PALB2 sequence variants.

American journal of human genetics·2026
Same author

Genetic and physical interactions reveal overlapping and distinct contributions to meiotic double-strand break formation in <i>C. elegans</i>.

eLife·2026
Same author

Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus.

Molecular cell·2026
Same author

Pathogenic Germline PALB2 and RAD50 Variants in Patients With Relapsed Ewing Sarcoma.

Pediatric blood & cancer·2026
Same journal

Erratum for Yamamoto et al., Novel 44-Kilodalton Subunit of Axonemal Dynein Conserved from <i>Chlamydomonas</i> to Mammals.

Eukaryotic cell·2017
Same journal

Correction for Liang et al., A Novel Function for Hog1 Stress-Activated Protein Kinase in Controlling White-Opaque Switching and Mating in Candida albicans.

Eukaryotic cell·2016
Same journal

Retraction for Chavez-Dozal et al. Functional Analysis of the Exocyst Subunit Sec15 in Candida albicans.

Eukaryotic cell·2016
Same journal

Retraction for Chavez-Dozal et al., The Candida albicans Exocyst Subunit Sec6 Contributes to Cell Wall Integrity and Is a Determinant of Hyphal Branching.

Eukaryotic cell·2016
Same journal

The New Shape of EC.

Eukaryotic cell·2015
Same journal

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis.

Eukaryotic cell·2015
See all related articles

The small-subunit (SSU) processome, crucial for 18S rRNA biogenesis, has 12 new protein components identified. This discovery links rRNA processing and ribosome assembly, revealing new roles for ribosomal proteins.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The small-subunit (SSU) processome is a large ribonucleoprotein complex essential for 18S ribosomal RNA (rRNA) biogenesis.
  • It is implicated in the terminal structures observed on nascent rRNAs during electron microscopy.
  • Previous studies identified 28 protein components in the Saccharomyces cerevisiae SSU processome.

Purpose of the Study:

  • To characterize additional protein components of the SSU processome.
  • To investigate the functional roles of identified proteins in rRNA processing and ribosome assembly.
  • To expand the understanding of the molecular machinery involved in ribosome biogenesis.

Main Methods:

  • Co-immunoprecipitation assays using Mpp10 and U3 small nucleolar RNA (snoRNA).

Related Experiment Videos

  • Analysis of anticipated pre-ribosomal RNA (pre-rRNA) interactions.
  • Characterization of protein components based on established criteria for bona fide SSU processome members.
  • Main Results:

    • Twelve new protein components were identified in the SSU processome.
    • Five of these are small-ribosomal-subunit proteins (Rps4, Rps6, Rps7, Rps9, and Rps14).
    • Seven other proteins (Utp18, Noc4, Utp20, Utp21, Utp22, Emg1, and Krr1) were confirmed as bona fide SSU processome components.

    Conclusions:

    • The SSU processome plays a role in both pre-rRNA processing and ribosome assembly.
    • The identified ribosomal proteins may function similarly to bacterial RNA-binding proteins in ribosome assembly.
    • This study significantly expands the known composition and potential functions of the SSU processome.