Abstract
Rice root proteomics research identified to a new remorin1 protein,named OsREM1,which significantly increased (approximately 1.7-fold) compared with control under salt stress by Two-dimensional electrophoresis. It is found that the protein molecular weight is 29 kD, isoelectric point is 4.54. The bioinformatics analysis showed that: (1) The protein contains 195 amino acids, whose theoretical molecular weight is 21.3 kD, whose theoretical isoelectric point is 5.06. There are some differences with the experimental results, which may be the result of post-translational modification, such as glycosylation, phosphorylation; (2) The different crop remorin protein sequence alignment analysis found that the same rate of the amino acids is more than 50%, indicated that remorins are highly conserved protein; (3) Phylogenetic analysis showed OsREM1 had a low sequence identity with potao and tomato REM1, which is the agreement with traditional classification.
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