Detection of discriminative sequence motifs in proteins obtained from prokaryotes grown at various temperatures.
Recent investigations on the stability of proteins have demonstrated various structural factors, but few have considered sequence factors such as protein motifs. These motifs represent highly conserved regions and describe critical regions that may only exist on proteins that remain functional at high temperatures. This investigation presents a method for identifying and comparing corresponding mesophilic and thermophilic sequence motifs between protein families. Discriminative motifs that are conserved only in the mesophilic or thermophilic subfamily are identified. Analysis of the results shows that, although the subfamilies of most protein families share similar motifs, some discriminative motifs are present in particular thermophilic/mesophilic subfamilies. The thermophilic discriminative motifs are conserved only in thermophilic organisms, revealing that physiochemical principles support thermostability.
Department of Computer Science and Information Engineering, National Central University, Taiwan, Republic of China.
Li-Cheng
LC
Wu
Jorng-Tzong
JT
Horng
Shir-Ly
SL
Huang
Hsien-Da
HD
Huang
Baw-Jhiune
BJ
Liu
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D007477:Ions / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D013696:Temperature
D007477:Ions; D011506:Proteins