Investigation of the molecular mechanism of the putative histone reader function of the NSD histone methyltransferase family.

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The combination of posttranslational modifications of histones the histone code has been implicated in the regulation of gene expression. So far it is hardly understood how the histone code is read and translated into downstream events. In contrast to many other proteins with domains able to read histone modifications (histone reader domains), the NSD protein family has a unique compact cluster of six histone reader domains. Single point mutations at multiple positions within this cluster leads to a dysfunctional enzyme, indicating that this cluster functions as a unit, where each single domain is indispensable. I propose to study the putative histone reader function of this specialized unit, to gain insights into the mechanism how a certain histone code is read by the combined action of several histone reader domains. Understanding the mechanisms of such a prototypic histone reader might raise the possibility to create customized histone readers, recognizing other histone modification combinations. These artificial histone readers could become valuable and versatile tools in research and medicine.