Expression, in vivo localization and phylogenetic analysis of a pyridoxine 5′-phosphate oxidase in Arabidopsis thaliana

被引:27
|
作者
Sang, Yuying [1 ]
Locy, Robert D. [1 ]
Goertzen, Leslie R. [1 ]
Rashotte, Aaron M. [1 ]
Si, Ying [2 ]
Kang, Kwonkyoo [3 ]
Singh, Narendra K. [1 ]
机构
[1] Auburn Univ, Dept Biol Sci, Auburn, AL 36849 USA
[2] Auburn Univ, Dept Hort, Auburn, AL 36849 USA
[3] Hankyong Natl Univ, Dept Hort, Seoul, South Korea
关键词
Arabidopsis thaliana; Pyridox_oxidase domain; Yjef_N domain; Chloroplast localization; RNAi mutants; VITAMIN-B-6; BIOSYNTHESIS; GENE; STRESS; MUTANT; SENSITIVITY; RESISTANCE; TOLERANCE; RESPONSES; SEQUENCE; PDX1;
D O I
10.1016/j.plaphy.2010.10.003
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Pyridoxal phosphate (PLP), a vitamin B-6 vitamer, is an essential cofactor for numerous enzymes. Pyridoxine/pyridoxamine phosphate oxidase (PPOX) catalyzes the synthesis of pyridoxal phosphate from pyridoxine phosphate (PNP) and/or pyridoxamine phosphate (PMP). The Ar5g49970 locus in Arabidopsis thaliana encodes an AtPPOX, a PNP/PMP oxidase. The expression of the AtPPOX gene varied in different tissues of Arabidopsis examined, being up-regulated by light, heat shock, ABA, and ethylene treatments, and down-regulated by exposure to drought and NaCl. Monoclonal antibodies raised against two different domains of AtPPOX recognized different sizes of AtPPOX, suggesting that AtPPOX proteins are produced as splice variants of the AtPPOX gene in Arabidopsis. Phylogenetic analysis of AtPPOX across all domains of life demonstrated that plant AtPPOX homologs have an additional Yjef_N domain preceding the Pyridox_Oxidase domain at the C-terminal end of the protein, while AtPPOX homologs from bacteria, fungi and animals have only Pyridox_Oxidase domain. The presence of the Yjef_N domain in plant AtPPOX homologs suggests that acquisition of this domain, and its fusion with the pyridox_oxidase domain began with the endosymbiotic acquisition of the chloroplast. Bioinformatic analysis suggested that AtPPOX is localized in chloroplast, but the monoclonal antibody could not be used for subcellular localization of this protein. A GFP-AtPPOX fusion construct introduced into the Arabidospsis protoplast confirmed localization of AtPPOX into the chloroplast. An RNAi mutant of AtPPOX showed sensitivity to high light suggesting a role for PPOX in resistance to photooxidative damage, and alteration in root growth in the presence of sucrose suggests a role for PPOX in root development. Published by Elsevier Masson SAS.
引用
收藏
页码:88 / 95
页数:8
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