title: Proteome approach to characterize the methylmalonate-semialdehyde dehydrogenase that is regulated by gibberellin.
abstract: Proteins regulated by gibberellin (GA) in rice were determined by proteome analysis. Proteins extracted from suspension culture cells of slr1, a constitutive GA response mutant of rice, were separated by two-dimensional polyacrylamide gel electrophoresis, and three proteins were greatly accumulated in the mutant. The most up-regulated protein was methylmalonate-semialdehyde dehydrogenase (MMSDH), and the amount of protein was 7-fold that of wild type. In this study, the function of MMSDH in rice was analyzed. MMSDH gene expression in suspension culture cells, roots, and leaf sheaths ofslr1 was higher than that in its wild-type. MMSDH expression in wild-type roots was increased by exogenous GA(3). Analyzed by in situ hybridization, MMSDH mRNA was expressed in root primordia of slr1, where cells are undergoing growth. MMSDH gene expression in the root zone of tissue differentiation was higher than in the elongation zone or meristem. Transgenic rice expressing antisense MMSDH showed that its seminal roots were thinner than that of control, and that the leaf sheath elongation was slightly inhibited compared to control. Concentrations of TCA cycle metabolites were decreased in the antisense plants as compared with the control plants, suggesting that acetyl-CoA was reduced in the antisense plants. These results suggest that one of the regulations by GA signal transduction including SLR1 is the expression of MMSDH, and that MMSDH may play a role in root development and leaf sheath elongation in rice.
authors.affiliation: Department of Molecular Genetics, National Institute of Agrobiological Sciences, Tsukuba 305-8602, Japan.
authors.forename: Naoki
authors.initials: N
authors.lastname: Tanaka
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Takahashi
authors.forename: Hidemi
authors.initials: H
authors.lastname: Kitano
authors.forename: Makoto
authors.initials: M
authors.lastname: Matsuoka
authors.forename: Shoichiro
authors.initials: S
authors.lastname: Akao
authors.forename: Hirofumi
authors.initials: H
authors.lastname: Uchimiya
authors.forename: Setsuko
authors.initials: S
authors.lastname: Komatsu
mesh_terms: D015180:Electrophoresis, Gel, Two-Dimensional; D005786:Gene Expression Regulation; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D005822:Genetic Vectors; D005875:Gibberellins / Q000737:chemistry* / Q000378:metabolism; D017403:In Situ Hybridization; D050646:Methylmalonate-Semialdehyde Dehydrogenase (Acylating) / Q000737:chemistry*; D008957:Models, Genetic; D009154:Mutation; D016376:Oligonucleotides, Antisense / Q000737:chemistry; D012275:Oryza / Q000201:enzymology* / Q000235:genetics*; D010449:Peptide Mapping; D010641:Phenotype; D018515:Plant Leaves / Q000378:metabolism; D010944:Plants / Q000378:metabolism; D030821:Plants, Genetically Modified; D011506:Proteins / Q000737:chemistry; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D012313:RNA / Q000737:chemistry; D012333:RNA, Messenger / Q000378:metabolism; D012335:RNA, Ribosomal / Q000737:chemistry; D015398:Signal Transduction; D013997:Time Factors; D019076:Transgenes; D015854:Up-Regulation
chemical_list: D005875:Gibberellins; D016376:Oligonucleotides, Antisense; D011506:Proteins; D020543:Proteome; D012333:RNA, Messenger; D012335:RNA, Ribosomal; D012313:RNA; D050646:Methylmalonate-Semialdehyde Dehydrogenase (Acylating)