Abstract:
:We report the results of a chemogenomic profiling aimed to explore the mode of action of a quinolic analogue of the p300 histone acetyltransferase (HAT) inhibitor anacardic acid, named MC1626. This compound reduced histone H3 acetylation in a dose-dependent manner and the HATs Gcn5 and Rtt109, which specifically target H3 lysines, were the only ones that caused chemical-genetic synthetic sickness with MC1626 when mutated. Deletion of specific Gcn5 (e.g., Ada1) and Rtt109 (e.g., Asf1) multiprotein complex components also enhanced MC1626 sensitivity. In addition to N-terminal H3 lysines, MC1626 inhibits H3-K56 acetylation, a histone modification that, in yeast, is exclusively supported by Rtt109 and indirectly influences DNA integrity. Several DNA repair mutants were found to be sensitive to MC1626. Functional links between histone acetylation impairment by MC1626 and mitochondrion as well as cytoskeleton functionality were also revealed, thus extending the range of non-nuclear processes that are influenced by histone acetylation.
journal_name
Genomicsjournal_title
Genomicsauthors
Ruotolo R,Tosi F,Vernarecci S,Ballario P,Mai A,Filetici P,Ottonello Sdoi
10.1016/j.ygeno.2010.08.005subject
Has Abstractpub_date
2010-11-01 00:00:00pages
272-80issue
5eissn
0888-7543issn
1089-8646pii
S0888-7543(10)00180-1journal_volume
96pub_type
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