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MBC in Press, published online ahead of print January 23, 2004
Mol. Biol. Cell 10.1091/mbc.E03-08-0623

A more recent version of this article appeared on April 1, 2004
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Submitted on August 25, 2003
Revised on December 17, 2003
Accepted on January 8, 2004

NO66 - a highly conserved dual location protein in the nucleolus and in a special type of synchronously replicating chromatin

Jens Eilbracht1, Michaela Reichenzeller1, Michaela Hergt1, Martina Schnölzer2, Hans Heid1, Michael Stöhr3, Werner W. Franke1, and Marion S. Schmidt-Zachmann1*

1 Division of Cell Biology, German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany
2 Protein Analysis Facility, German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany
3 Cytometry Facility, German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany

* Corresponding author. E-mail address: m.schmidt-zachmann{at}dkfz.de.

It has recently become clear that the nucleolus, the most prominent nuclear subcompartment, harbors diverse functions beyond its classic role in ribosome biogenesis. To gain insight into nucleolar functions, we have purified amplified nucleoli from Xenopus laevis oocytes using a novel approach involving fluorescence-activated cell sorting (FACS) techniques. The resulting protein fraction was analyzed by mass spectrometry and used for the generation of monoclonal antibodies directed against nucleolar components. Here, we report the identification and molecular characterization of a novel, ubiquitous protein which in most cell types appears to be a constitutive nucleolar component. Immunolocalization studies have revealed that this protein, termed NO66, is highly conserved during evolution and shows in most cells analyzed a dual localization pattern, i.e., a strong enrichment in the granular part of nucleoli and in distinct nucleoplasmic entities. Colocalizations with proteins Ki-67, HP1{alpha} and PCNA, respectively, have further shown that the staining pattern of NO66 overlaps with certain clusters of late replicating chromatin. Biochemical experiments have revealed that protein NO66 cofractionates with large preribosomal particles but is absent from cytoplasmic ribosomes. We propose that in addition to its role in ribosome biogenesis protein NO66 has functions in the replication or remodeling of certain heterochromatic regions.




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