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Structure and function of histone acetyltransferase complexes in Arabidopsis thaliana
Author(s) -
Tedesco Dana C.,
Lord Nathan,
Triezenberg Steven J.,
Hark Amy T.
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.892.3
Subject(s) - arabidopsis , histone acetyltransferase , histone acetyltransferases , biology , chromatin , arabidopsis thaliana , coactivator , acetyltransferase , genetics , histone , acetylation , gene , p300 cbp transcription factors , microbiology and biotechnology , mutant , transcription factor
The structure of chromatin plays a crucial role in eukaryotic gene regulation. In response to chemical and environmental stresses or developmental signals, nucleosomes can be modified by histone acetyltransferases (HATs) to affect transcription. The Spt‐ADA2‐GCN5 acetyltransferase complex (SAGA) with its characteristic HAT activity participates in chromatin modification in humans, Drosophila, and yeast. Homologous genes encoding the HAT GCN5 and the coactivator ADA2 have been identified in Arabidopsis thaliana , but SAGA‐related protein complexes in plants have not yet been described. To better understand potential biochemical interactions between ADA2b, GCN5, and other components in histone acetylation in Arabidopsis , we are testing the functions of specific domains of Arabidopsis ADA2b. As one example, a construct harboring a deletion of a plant‐specific domain was introduced into an ada2b‐1 mutant background and transgenic lines will be assessed for phenotypic rescue. In addition, TAP‐tagged ADA2b lines ( ada2b‐1−/−;35S:ADA2bcTAPi ) were established that will be employed to characterize biochemical interactions of ADA2b and define the components of a putative Arabidopsis SAGA complex. This work was supported by MERCK/AAAS, Muhlenberg College, and National Science Foundation grant MCB‐0240309.