Comparative structural analysis of HAC1 in Arabidopsis thaliana

• Main Authors: Amar Cemanovic, Jasmin Sutkovic, Mohamed Ragab Abdel Gawwad
• Format: Article
• Language: English
• Published: International Academy of Ecology and Environmental Sciences 2014-06-01
• Series: Network Biology
• Subjects: Arabidopsis thaliana; HAC1 protein; 3-D structure; structure prediction; homology
• Online Access: http://www.iaees.org/publications/journals/nb/articles/2014-4(2)/comparative-structural-analysis-of-HAC1-in-Arabidopsis-thaliana.pdf
• ISSN: 2220-8879; 2220-8879

Histone acetylation is an important posttranslational modification correlated with gene activation. In Arabidopsis thaliana, the histone acetyltransferase 1 (AtHAC1) is homologous to animal p300/CREB (cAMPresponsive element-binding protein)-binding proteins, which are the main histone acetyltransferases participating in many physiological processes, including proliferation, differentiation, and apoptosis. In this study the 3-D structure of the HAC1 protein in Arabidopsis thaliana was predicted using 4 homology-based prediction servers: ESyPred3D, 3D-JIGSAW, SWISS-MODEL and PHYRE2. The homology modeled structureswere evaluated and stereochemical analysis done by Ramachadran plot analysis. The amino acid sequences of Arabidopsis thaliana HAC1 protein are highly similar to the sequence of the homologous human p300/CREB. SWISS MODEL and Phyre2 servers computed the identical 3D structures. Validation and verification methods, using Z-score and 3D-1D score, showed that these 3D models are of good and acceptable quality.