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Updated: Aug 14, 2026

Quantitative Analysis of Chromatin Proteomes in Disease
Published on: December 28, 2012
Directed proteomic analysis of the human nucleolus
Jens S Andersen1, Carol E Lyon, Archa H Fox
1Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230, Odense M, Denmark.
This study reveals the nucleolus has more proteins than previously known, including many from uncharacterized genes. Nucleolar protein composition is dynamic and changes with cell metabolism.
Area of Science:
- Cell Biology
- Proteomics
Background:
- The nucleolus is a key subnuclear structure involved in ribosome biogenesis.
- Emerging evidence suggests nucleoli play roles in RNA transport, modification, and cell cycle regulation.
- Despite extensive research, nucleolar structure and function are not fully understood.
Purpose of the Study:
- To conduct a comprehensive proteomic analysis of human nucleoli.
- To identify the full spectrum of proteins within the nucleolus.
- To investigate the dynamic nature of the nucleolar proteome.
Main Methods:
- Proteomic analysis using mass spectrometry (MS).
- Sequence database searches, including analysis of the draft human genome.
- Isolation of nucleoli from HeLa cells with inhibited transcription.
Main Results:
- Identified 271 proteins in human nucleoli.
- Over 30% of identified proteins were encoded by novel or uncharacterized genes.
- Observed enrichment of specific proteins under transcription inhibition, indicating dynamic association.
Conclusions:
- Human nucleoli possess greater protein complexity than previously recognized.
- Novel proteins and diverse protein classes suggest additional nucleolar functions beyond ribosome biogenesis.
- Nucleolar protein composition is dynamic and responsive to cellular metabolic state.
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