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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Volume 388, Issue 9 (Sep 2007)


Sumoylation of the zinc finger protein ZXDC enhances the function of its transcriptional activation domain

Srikarthika Jambunathan
  • 1Department of Biological, Geological and Environmental Sciences, Cleveland State University, Cleveland, OH 44115, USA
/ Joseph D. Fontes
  • 2Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA
Published Online: 2007-08-14 | DOI: https://doi.org/10.1515/BC.2007.106


The transcription of major histocompatibility complex class II (MHC II) genes is dependent on the co-activator protein class II trans-activator (CIITA). We have recently identified a protein known as zinc finger X-linked duplicated family member C (ZXDC) that, along with its binding partner ZXDA, forms a complex that interacts with CIITA and regulates MHC II transcription. Western blot analysis with anti-ZXDC antibodies identified two species of the ZXDC protein, one migrating near its predicted molecular mass and one with slower electrophoretic mobility. We report here that the slower migrating form is the result of sumoylation at a single lysine residue within the transcriptional activation domain of ZXDC. Three SUMO proteins (SUMO-1, -2 and -3) can modify the ZXDC protein. Multiple SUMO E3 ligase enzymes and HDAC4 can facilitate ZXDC sumoylation, and one ligase, PIASy, interacts with a specific region of the ZXDC protein. We found that sumoylation does not appear to disrupt or modulate the interaction of ZXDC with its binding partners. Rather, sumoylation of ZXDC is required for full activity of the transcriptional activation domain. Our findings suggest that sumoylation is an important regulator of ZXDC.

Keywords: gene transcription; histocompatibility; sumoylation; zinc finger

About the article

Corresponding author

Received: 2007-04-10

Accepted: 2007-05-24

Published Online: 2007-08-14

Published in Print: 2007-09-01

Citation Information: Biological Chemistry, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.106. Export Citation

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