dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

Roman Kessler, Johan Tisserand, Joan Font-Burgada, Oscar Reina, Laura Coch, Camille Stephan-otto Attolini, Ivan Garcia-Bassets and Fernando Azorín ()
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Roman Kessler: Institute of Molecular Biology of Barcelona, CSIC
Johan Tisserand: Institute of Molecular Biology of Barcelona, CSIC
Joan Font-Burgada: Institute of Molecular Biology of Barcelona, CSIC
Oscar Reina: Institute for Research in Biomedicine, IRB Barcelona
Laura Coch: Institute of Molecular Biology of Barcelona, CSIC
Camille Stephan-otto Attolini: Institute for Research in Biomedicine, IRB Barcelona
Ivan Garcia-Bassets: School of Medicine, University of California, San Diego
Fernando Azorín: Institute of Molecular Biology of Barcelona, CSIC

Nature Communications, 2015, vol. 6, issue 1, 1-14

Abstract: Abstract dDsk2 is a conserved extraproteasomal ubiquitin receptor that targets ubiquitylated proteins for degradation. Here we report that dDsk2 plays a nonproteolytic function in transcription regulation. dDsk2 interacts with the dHP1c complex, localizes at promoters of developmental genes and is required for transcription. Through the ubiquitin-binding domain, dDsk2 interacts with H2Bub1, a modification that occurs at dHP1c complex-binding sites. H2Bub1 is not required for binding of the complex; however, dDsk2 depletion strongly reduces H2Bub1. Co-depletion of the H2Bub1 deubiquitylase dUbp8/Nonstop suppresses this reduction and rescues expression of target genes. RNA polymerase II is strongly paused at promoters of dHP1c complex target genes and dDsk2 depletion disrupts pausing. Altogether, these results suggest that dDsk2 prevents dUbp8/Nonstop-dependent H2Bub1 deubiquitylation at promoters of dHP1c complex target genes and regulates RNA polymerase II pausing. These results expand the catalogue of nonproteolytic functions of ubiquitin receptors to the epigenetic regulation of chromatin modifications.

Date: 2015
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DOI: 10.1038/ncomms8049

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