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2. Functional analysis of histone deacetylase RPD3/HDA1 family in Physcomitrella patens by bioinformatics

Author

Zhengbin Chen, Jinmei Fu, Wenqun Fu, Li Li, Xiaoling Teng, Ying Lin, Yuling Wang, and Xiaoqing Li

Subjects
Signal peptide, Biochemistry, biology, Transcriptional regulation, Chromatin silencing, Histone deacetylase, Casein kinase 2, Bioinformatics, Physcomitrella patens, biology.organism_classification, Transmembrane protein, Protein kinase C
Abstract

The biological function of RPD3/HDA1 HDACs family from Physcomitrella patens was investigated by using bioinformatics. The results showed that the members of RPD3/HDA1 HDACs family were localized in different subcellular localization of P. patens, and their encoding proteins all have four sites, such as the protein kinase C phosphorylation site, the Casein kinase II phosphorylation site, the N-glycosylation site, and the N-myristoylation site. The RPD3/HDA1 HDACs members all have no transmembrane regions and they are hydrophilic proteins without signal peptide. The RPD3/HDA1 HDACs members from P. patens were aligned by ClustalW2 and their HDACs domains are highly conserved. These RPD3/HDA1 HDACs seemed to be involved in processes, such as transcription regulation, energy metabolism and chromatin silencing in P. patens.

Published
2011
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