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Updated: Jul 13, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
The multifunctional human p100 protein 'hooks' methylated ligands.
Neil Shaw1, Min Zhao, Chongyun Cheng
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
The human p100 protein acts as a transcription regulator. Its tudor and SN domain interacts with snRNP complexes, revealing a role in RNA splicing and transcription.
Area of Science:
- Molecular Biology
- Structural Biology
- Gene Regulation
Background:
- The human p100 protein is a key regulator of gene transcription.
- It bridges promoter-specific activators and basal transcription machinery.
Purpose of the Study:
- To investigate the interaction of the p100 protein's tudor and SN (TSN) domain with U small nuclear ribonucleoprotein (snRNP) complexes.
- To elucidate the structural basis of p100's function in transcription and RNA processing.
Main Methods:
- X-ray crystallography to determine the structure of the p100 TSN domain.
- Biochemical assays to analyze protein interactions.
Main Results:
- The p100 TSN domain structure resembles a hook with a hinge mechanism.
- A conserved aromatic cage within the TSN domain binds methyl groups of snRNPs.
- This interaction anchors p100 to the spliceosome, suggesting a role in precursor messenger RNA processing.
Conclusions:
- The p100 protein plays a dual role in both gene transcription and RNA splicing.
- Structural insights into the TSN domain explain its molecular interactions with snRNPs and the spliceosome.
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