Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of

Document Type

Article

Publication Version

Published Version

Publication Date

4-6-2010

Journal or Book Title

PloS ONE

Volume

5

Issue

4

First Page

e10042

DOI

10.1371/journal.pone.0010042

Abstract

The histone methyltransferase SU(VAR)3–9 plays an important role in the formation of heterochromatin within the eukaryotic nucleus. Several studies have shown that the formation of condensed chromatin is highly regulated during development, suggesting that SU(VAR)3–9's activity is regulated as well. However, no mechanism by which this may be achieved has been reported so far. As we and others had shown previously that the N-terminus of SU(VAR)3–9 plays an important role for its activity, we purified interaction partners from Drosophila embryo nuclear extract using as bait a GST fusion protein containing the SU(VAR)3–9 N-terminus. Among several other proteins known to bind Su(VAR)3–9 we isolated the chromosomal kinase JIL-1 as a strong interactor. We show that SU(VAR)3–9 is a substrate for JIL-1 in vitro as well as in vivo and map the site of phosphorylation. These findings may provide a molecular explanation for the observed genetic interaction between SU(VAR)3–9 and JIL-1.

Comments

This article is published as Boeke J, Regnard C, Cai W, Johansen J, Johansen KM, Becker PB, et al. (2010) Phosphorylation of SU(VAR)3–9 by the Chromosomal Kinase JIL-1. PLoS ONE 5(4): e10042. doi: 10.1371/journal.pone.0010042.

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

Copyright Owner

Boeke et al.

Language

en

File Format

application/pdf

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