Differential regulation of proteins and phosphoproteins in rice under drought stress.
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.
Ke
Yuqin
Y
Key Laboratory of Ministry of Education for Genetic, Breeding and Multiple Utilization of Crops, Fuzhou, China.
Han
Guoqiang
G
He
Huaqin
H
Li
Jiaxu
J
D055864:Droughts; D018506:Gene Expression Regulation, Plant; D012275:Oryza / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D010446:Peptide Fragments / Q000737:chemistry; D010750:Phosphoproteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D010766:Phosphorylation; D040901:Proteomics; D013312:Stress, Physiological / Q000235:genetics; D014357:Trypsin / Q000737:chemistry
D010446:Peptide Fragments; D010750:Phosphoproteins; D014357:Trypsin