Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
 QUICK SEARCH:   [advanced]


     


MBC in Press, published online ahead of print May 28, 2004
Mol. Biol. Cell 10.1091/mbc.E04-03-0253

A more recent version of this article appeared on August 1, 2004
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E04-03-0253v1
15/8/3876    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Saitoh, N.
Right arrow Articles by Spector, D. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Saitoh, N.
Right arrow Articles by Spector, D. L.

Submitted on March 25, 2004
Revised on May 20, 2004
Accepted on May 20, 2004

Proteomic Analysis of Interchromatin Granule Clusters

Noriko Saitoh*{dagger}, Chris S. Spahr{ddagger}, Scott Patterson{ddagger}, Paula Bubulya*, Andrew F. Neuwald*, and David L. Spector*{sect}

*Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724; and {ddagger}Amgen Center, Thousand Oaks, California 91320-1789

Monitoring Editor: Joseph Gall

A variety of proteins involved in gene expression have been localized within mammalian cell nuclei in a speckled distribution that predominantly corresponds to interchromatin granule clusters (IGCs). We have applied a mass spectrometry strategy to identify the protein composition of this nuclear organelle purified from mouse liver nuclei. Using this approach we have identified 146 proteins, many of which had already been shown to be localized to IGCs, or their functions are common to other already identified IGC proteins. In addition, we identified 32 proteins for which only sequence information is available and thus these represent novel IGC protein candidates. We find that 54% of the identified IGC proteins have known functions in pre-mRNA splicing. In combination with proteins involved in other steps of pre-mRNA processing, 81% of the identified IGC proteins are associated with RNA metabolism. In addition, proteins involved in transcription, as well as several other cellular functions, have been identified in the IGC fraction. However, the predominance of pre-mRNA processing factors supports the proposed role of IGCs as assembly, modification and/or storage sites for proteins involved in pre-mRNA processing.


{dagger}Present address: Department of Regeneration Medicine, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Kumamoto-shi, Kumamoto 860-0811, Japan

{sect}Corresponding author.

David L. Spector, E-mail: spector{at}cshl.org







Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.