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Related Experiment Video

Updated: Jul 19, 2026

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

Extraction of nuclear proteins.

Setsuko Komatsu¹

¹Laboratory of Gene Regulation, Department of Molecular Genetics, National Institute of Agrobiological Sciences, Tsukuba, Japan.

Methods in Molecular Biology (Clifton, N.J.)

|November 10, 2006

Summary

Researchers developed a rapid and efficient method for isolating high-purity plant nuclei. This technique ensures nuclear protein integrity for accurate subcellular proteome studies.

Area of Science:

Plant Cell Biology
Subcellular Proteomics

Background:

Accurate analysis of subcellular proteomes, like the nucleus, requires high-purity isolated compartments.
Plant nuclear isolation is challenging due to cellular contaminants.

Purpose of the Study:

To establish a rapid and efficient method for isolating high-purity nuclei from cultured rice suspension cells.
To prepare nuclear proteins from purified nuclei for further analysis.

Main Methods:

Modified sucrose density gradient centrifugation for nuclear isolation.
Preparation of nuclear proteins using lysis buffer or SDS sample buffer.
Western blot analysis with anti-histone H1 antibody to assess purity.

Main Results:

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The modified sucrose gradient method proved more rapid and efficient than previous techniques.

Isolated nuclei were uniform spheres with an average diameter of approximately 20 micrometers.

Western blot confirmed the presence of histone H1 exclusively in the nuclear fraction, indicating high purity.

Conclusions:

The developed method successfully isolates high-purity plant nuclei.
This technique is crucial for reliable studies of nuclear proteins and subcellular proteomes in plants.