Abstract:

Multiple alignment of amino acid sequences of CRT-binding factor1(CBF1) from 18 different plants was conducted and a phylogenetic tree with these proteins was built.In addition,the characters of the amino acid constitutions,isoelectric point,hydrophilic/hydrophobic properties,secondary structures,tertiary structures and functional domains of these proteins were analyzed with the tools of bioinformatics software.The results showed that nuclear localization signals(NLS) were rich in Argnine(Arg) and Lysine(Lys) residues at N-terminal of CBF1 in 18 different plants,while containing AP2 core domains which bind to DNA and acidic amino acids were located in C-terminal.Molecular evolution was analyzed by cladogram construction of CBF1.Amino acids of CBF1 mainly belonged to aliphatic series.All CBF1s in 18 different plants contained non-polar amino acid Ala,and most of the isoelectric points were acid,the proteins of CBF1 were unstable and hydrophilic.Constructions of α-helixs and random coils in CBF1 were dominant elements from 18 different plants,β-turns and extended strains interspersed over the whole proteins.Subcellular localizations of CBF1 protein were different.A three-dimensional structure test validated that the modeling accorded with the stereochemistry.This study provides basic information for the research of gene structure and biological function,and also provides evidence for the analysis of the function of interaction in different signal pathway and regulating mechanism.

Key words: CRT-binding factor, bioinformatics, molecular evolution