title: Proteome analysis of the wild and YX-1 male sterile mutant anthers of wolfberry (Lycium barbarum L.).
abstract: Pollen development is disturbed in the early tetrad stage of the YX-1 male sterile mutant of wolfberry (Lycium barbarum L.). The present study aimed to identify differentially expressed anther proteins and to reveal their possible roles in pollen development and male sterility. To address this question, the proteomes of the wild-type (WT) and YX-1 mutant were compared. Approximately 1760 protein spots on two-dimensional differential gel electrophoresis (2D-DIGE) gels were detected. A number of proteins whose accumulation levels were altered in YX-1 compared with WT were identified by mass spectrometry and the NCBInr and Viridiplantae EST databases. Proteins down-regulated in YX-1 anthers include ascorbate peroxidase (APX), putative glutamine synthetase (GS), ATP synthase subunits, chalcone synthase (CHS), CHS-like, putative callose synthase catalytic subunit, cysteine protease, 5B protein, enoyl-ACP reductase, 14-3-3 protein and basic transcription factor 3 (BTF3). Meanwhile, activities of APX and GS, RNA expression levels of apx and atp synthase beta subunit were low in YX-1 anthers which correlated with the expression of male sterility. In addition, several carbohydrate metabolism-related and photosynthesis-related enzymes were also present at lower levels in the mutant anthers. In contrast, 26S proteasome regulatory subunits, cysteine protease inhibitor, putative S-phase Kinase association Protein 1(SKP1), and aspartic protease, were expressed at higher levels in YX-1 anthers relative to WT anthers. Regulation of wolfberry pollen development involves a complex network of differentially expressed genes. The present study lays the foundation for future investigations of gene function linked with wolfberry pollen development and male sterility.
authors.affiliation: National Key Laboratory of Crop Genetics and Germplasm Enhancement, National Center for Soybean Improvement, Nanjing Agricultural University, Nanjing, China.
authors.forename: Rui
authors.initials: R
authors.lastname: Zheng
authors.lastname: Sijun Yue
authors.forename: Xiaoyan
authors.initials: X
authors.lastname: Xu
authors.forename: Jianyu
authors.initials: J
authors.lastname: Liu
authors.forename: Qing
authors.initials: Q
authors.lastname: Xu
authors.forename: Xiaolin
authors.initials: X
authors.lastname: Wang
authors.forename: Lu
authors.initials: L
authors.lastname: Han
authors.forename: Deyue
authors.initials: D
authors.lastname: Yu
mesh_terms: D025181:ATP Synthetase Complexes / Q000378:metabolism; D060387:Ascorbate Peroxidases / Q000378:metabolism; D035264:Flowers / Q000166:cytology / Q000235:genetics / Q000378:metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D032305:Lycium / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D058977:Molecular Sequence Annotation; D009154:Mutation; D010940:Plant Proteins / Q000378:metabolism*; D011058:Pollen / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D020543:Proteome / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D053719:Tandem Mass Spectrometry; D057825:Two-Dimensional Difference Gel Electrophoresis
chemical_list: D010940:Plant Proteins; D020543:Proteome; D060387:Ascorbate Peroxidases; D025181:ATP Synthetase Complexes; D005974:Glutamate-Ammonia Ligase