Background: Acetylation of core histones has been correlated with transcription, chromatin assembly, DNA repair, and recombinational events. Transfer of an acetyl group from acetyl–CoA onto the epsilon–amino group of different lysine residues in the NH2–terminal tail of core histones is a ubiquitous modification found in all euykaryotic species examined. Histone acetylation levels are controlled by the competing activities of histone acetyltransferases and histone deacetylases. Histone deacetylases are the catalytic subunits of multiprotein complexes that are targeted to specific promoters through their interaction with sequence–specific DNA–binding factors.
Description: Gladstone scientists have identified, cloned and characterized a novel human histone deacetylase (HDAC). This protein is highly expressed in specific populations of T lymphocytes in the thymus and at lower levels in other tissues. This newly discovered histone deacetylase is associated with histone deacetylase activity that is dependent on binding another identified histone deacetylase.
Applications: Since HDACs are involved in the control of gene regulation, HDAC genes are potential candidates as tumor suppressors. As such, their mutation could be associated with the development of cancers such as lymphomas, thymomas, or tumors of other organs. A probe of the newly discovered HDAC, or probes derived from its sequence, could become important tools for the diagnosis of specific cancers. Similarly, preparation and use of specific inhibitors of Gladstone’s newly discovered HDAC could play a significant role in the control of immunoproliferation, such as in immunosuppression for organ transplantation, as well as in the control of tumor development.
Reference: 2001-494
Gladstone Contact:
Caryl Cachola
Telephone: 415-734-2082
