Incorporating structural characteristics for identification of protein methylation sites.
Studies over the last few years have identified protein methylation on histones and other proteins that are involved in the regulation of gene transcription. Several works have developed approaches to identify computationally the potential methylation sites on lysine and arginine. Studies of protein tertiary structure have demonstrated that the sites of protein methylation are preferentially in regions that are easily accessible. However, previous studies have not taken into account the solvent-accessible surface area (ASA) that surrounds the methylation sites. This work presents a method named MASA that combines the support vector machine with the sequence and structural characteristics of proteins to identify methylation sites on lysine, arginine, glutamate, and asparagine. Since most experimental methylation sites are not associated with corresponding protein tertiary structures in the Protein Data Bank, the effective solvent-accessible prediction tools have been adopted to determine the potential ASA values of amino acids in proteins. Evaluation of predictive performance by cross-validation indicates that the ASA values around the methylation sites can improve the accuracy of prediction. Additionally, an independent test reveals that the prediction accuracies for methylated lysine and arginine are 80.8 and 85.0%, respectively. Finally, the proposed method is implemented as an effective system for identifying protein methylation sites. The developed web server is freely available at http://MASA.mbc.nctu.edu.tw/.
Shien
Dray-Ming
DM
Department of Computer Science and Information Engineering, National Central University, Chung-Li 320, Taiwan.
Lee
Tzong-Yi
TY
Chang
Wen-Chi
WC
Hsu
Justin Bo-Kai
JB
Horng
Jorng-Tzong
JT
Hsu
Po-Chiang
PC
Wang
Ting-Yuan
TY
Huang
Hsien-Da
HD
D001120:Arginine / Q000737:chemistry; D001216:Asparagine / Q000737:chemistry; D001665:Binding Sites; D003198:Computer Simulation; D018698:Glutamic Acid / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D008745:Methylation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013499:Surface Properties
D011506:Proteins; D018698:Glutamic Acid; D001216:Asparagine; D001120:Arginine; D008239:Lysine