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Abstract: Drought is the largest constraint on rice production in Asia. Protein phosphorylation has been recognized as an important mechanism for environmental stress signaling. However, the differential expression of proteins and phosphoproteins induced by drought in rice is still largely unknown. In this paper, we report the identification of differentially expressed proteins and phosphoproteins induced by drought in rice using proteomic approaches. Three drought-responsive proteins were identified. Late embryogenesis abundant (LEA)-like protein and chloroplast Cu–Zn superoxide dismutase (SOD) were up-regulated by drought whereas Rieske Fe–S precursor protein was down-regulated. Ten drought-responsive phosphoproteins were identified: NAD-malate dehydrogenase, OSJNBa0084K20.14 protein, abscisic acid- and stress-inducible protein, ribosomal protein, drought-induced S-like ribonuclease, ethylene-inducible protein, guanine nucleotide-binding protein beta subunit-like protein, r40c1 protein, OSJNBb0039L24.13 protein and germin-like protein 1. Seven of these phosphoproteins have not previously been reported to be involved in rice drought stress. These results provide new insight into the regulatory mechanism of drought-induced proteins and implicate several previously unrecognized proteins in response to drought stress. [Copyright &y& Elsevier]

Abstract: A rapid method to screen and identify unknown bound proteins to specific nucleic acid probes anchored on ProteinChip array surfaces from crude biological samples has been developed in this paper. It was demonstrated with screening specific binding proteins from LPS-stimulated mouse 70Z/3 pre-B cell nuclear extracts by direct coupling of thioaptamer XBY-S2 to the pre-activated ProteinChip array surfaces. With pre-fractionation of crude nuclear extracts by ion exchange method, specific “on-chip” captured proteins have been obtained that were pure enough to do “on-chip” digestion and the subsequent identification of the “on-chip” bound proteins by microsequencing of the trypsin digested peptide fragments through tandem MS. Five mouse heterogeneous nuclear ribonucleoproteins (hnRNPs) A1, A2/B1, A3, A/B, and D0 were identified. To verify those bound hnRNPs, a novel thioaptamer/antibody sandwich assay provides highly sensitive and selective identification of proteins on ProteinChip arrays. [Copyright &y& Elsevier]

In this paper, based on the approach by combining the “functional domain composition” [K.C. Chou, Y. D. Cai, J. Biol. Chem. 277 (2002) 45765] and the pseudo-amino acid composition [K.C. Chou, Proteins Struct. Funct. Genet. 43 (2001) 246; Correction Proteins Struct. Funct. Genet. 2044 (2001) 2060], the Nearest Neighbour Algorithm (NNA) was developed for predicting the protein subcellular location. Very high success rates were observed, suggesting that such a hybrid approach may become a useful high-throughput tool in the area of bioinformatics and proteomics. [Copyright &y& Elsevier]