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Network Biology, 2014, 4(3): 109-122
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3D structure prediction of histone acetyltransferase (HAC) proteins of the p300/CBP family and their interactome in Arabidopsis thaliana

Amar Cemanovic¹, Jasmin Sutkovic¹, Rabab Elamawi², Waleed Elkhoby², Mohamed Ragab Abdel Gawwad¹
¹Genetics and Bioengineering department, International University of Sarajevo, Ilidza, 71220 Bosnia and Herzegovina
²Rice Research and Training Center, Sakha, Egypt

Received 29 October 2013;Accepted 5 December 2013;Published online 1 September 2014
IAEES

Abstract
Histone acetylation is an important posttranslational modification correlated with gene activation. In Arabidopsis thaliana the histone acetyltransferase (HAC) proteins of the CBP family are homologous to animal p300/CREB (cAMP-responsive element-binding proteins, which are important histone acetyltransferases participating in many physiological processes, including proliferation, differentiation, and apoptosis. In this study the 3-D structure of all HAC protein subunits in Arabidopsis thaliana: HAC1, HAC2, HAC4, HAC5 and HAC12 is predicted by homology modeling and confirmed by Ramachandran plot analysis. The amino acid sequences HAC family members are highly similar to the sequences of the homologous human p300/CREB protein. Conservation of p300/CBP domains among the HAC proteins was examined further by sequence alignment and pattern search. The domains of p300/CBP required for the HAC function, such as PHD, TAZ and ZZ domains, are conserved in all HAC proteins. Interactome analysis revealed that HAC1, HAC5 and HAC12 proteins interact with S-adenosylmethionine-dependent methyltransferase domaincontaining protein that shows methyltransferase activity, suggesting an additional function of the HAC proteins. Additionally, HAC5 has a strong interaction value for the putative c-myb-like transcription factor MYB3R-4, which suggests that it also may have a function in regulation of DNA replication.

Keywords Arabidopsis thaliana;histone acetyltransferase;3D structure;interactome;functional annotation.

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