Aminopropyltransferases Involved in Polyamine Biosynthesis Localize Preferentially in the Nucleus of Plant Cells

被引:96
作者
Belda-Palazon, Borja [1 ]
Ruiz, Leticia [2 ]
Marti, Esmeralda [1 ]
Tarraga, Susana [1 ]
Tiburcio, Antonio F. [3 ]
Culianez, Francisco [1 ]
Farras, Rosa [4 ]
Carrasco, Pedro [5 ]
Ferrando, Alejandro [1 ]
机构
[1] Univ Politecn Valencia, CSIC, Inst Biol Mol & Celular Plantas, E-46071 Valencia, Spain
[2] Ctr Mojonera, Inst Andaluz Invest & Formac Agr, Almeria, Spain
[3] Univ Barcelona, Unidad Fisiol Vegetal, Barcelona, Spain
[4] Ctr Invest Principe Felipe, Valencia, Spain
[5] Univ Valencia, Dept Bioquim & Biol Mol, Valencia, Spain
来源
PLOS ONE | 2012年 / 7卷 / 10期
关键词
BIMOLECULAR FLUORESCENCE COMPLEMENTATION; SPERMIDINE SYNTHASE; ARABIDOPSIS-THALIANA; PROTEIN INTERACTIONS; CRYSTAL-STRUCTURE; S-ADENOSYLMETHIONINE; EXPRESSION; MECHANISM; ACYLTRANSFERASE; DECARBOXYLASE;
D O I
10.1371/journal.pone.0046907
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Plant aminopropyltransferases consist of a group of enzymes that transfer aminopropyl groups derived from decarboxylated S-adenosyl-methionine (dcAdoMet or dcSAM) to propylamine acceptors to produce polyamines, ubiquitous metabolites with positive charge at physiological pH. Spermidine synthase (SPDS) uses putrescine as amino acceptor to form spermidine, whereas spermine synthase (SPMS) and thermospermine synthase (TSPMS) use spermidine as acceptor to synthesize the isomers spermine and thermospermine respectively. In previous work it was shown that both SPDS1 and SPDS2 can physically interact with SPMS although no data concerning the subcellular localization was reported. Here we study the subcellular localization of these enzymes and their protein dimer complexes with gateway-based Bimolecular Fluorescence Complementation (BiFC) binary vectors. In addition, we have characterized the molecular weight of the enzyme complexes by gel filtration chromatography with in vitro assembled recombinant enzymes and with endogenous plant protein extracts. Our data suggest that aminopropyltransferases display a dual subcellular localization both in the cytosol and nuclear enriched fractions, and they assemble preferably as dimers. The BiFC transient expression data suggest that aminopropyltransferase heterodimer complexes take place preferentially inside the nucleus.
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页数:10
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