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Systematic identification and comparative analysis of lysine succinylation between the green and white parts of chimeric leaves of Ananas comosus var. bracteatus

Mao, Meiqin ; Xue, Yanbin ; He, Yehua ; Zhou, Xuzixing ; Rafique, Fatima ; Hu, Hao ; Liu, Jiawen ; Feng, Lijun ; Yang, Wei ; Li, Xi ; Sun, Lingxia ; Huang, Zhuo ; Ma, Jun

BMC genomics, 2020-06, Vol.21 (1), p.383-383, Article 383 [Periódico revisado por pares]

England: BioMed Central Ltd

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Título:
Systematic identification and comparative analysis of lysine succinylation between the green and white parts of chimeric leaves of Ananas comosus var. bracteatus
Autor: Mao, Meiqin ; Xue, Yanbin ; He, Yehua ; Zhou, Xuzixing ; Rafique, Fatima ; Hu, Hao ; Liu, Jiawen ; Feng, Lijun ; Yang, Wei ; Li, Xi ; Sun, Lingxia ; Huang, Zhuo ; Ma, Jun
Assuntos: Albinism ; Analysis ; Ananas - metabolism ; Ananas comosus ; Ananas comosus var ; bracteatus ; Breeding ; CAM photosynthesis ; Chimera - metabolism ; Chimeric leaves ; Chromatography, Liquid ; Citric acid ; Color ; Comparative analysis ; Crassulacean acid metabolism ; Energy metabolism ; Gene expression ; Gene Expression Regulation, Plant ; Genomics ; Glucose metabolism ; Glycolysis ; Immunohistochemistry ; Leaves ; Lysine ; Lysine - chemistry ; Lysine - metabolism ; Lysine succinylation ; Metabolism ; Peptides ; Phosphorylation ; Photorespiration ; Photosynthesis ; Physiological aspects ; Physiology ; Plant biochemistry ; Plant Leaves ; Plant Proteins - metabolism ; Post-translational modifications ; Protein Processing, Post-Translational ; Proteins ; Proteomics ; Pyruvic acid ; Succinic Acid - metabolism ; Tandem Mass Spectrometry ; Tricarboxylic acid cycle
É parte de: BMC genomics, 2020-06, Vol.21 (1), p.383-383, Article 383
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SourceType-Scholarly Journals-1
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Descrição: Lysine succinylation, an important protein posttranslational modification (PTM), is widespread and conservative. The regulatory functions of succinylation in leaf color has been reported. The chimeric leaves of Ananas comosus var. bracteatus are composed of normal green parts and albino white parts. However, the extent and function of lysine succinylation in chimeric leaves of Ananas comosus var. bracteatus has yet to be investigated. Compared to the green (Gr) parts, the global succinylation level was increased in the white (Wh) parts of chimeric leaves according to the Western blot and immunohistochemistry analysis. Furthermore, we quantitated the change in the succinylation profiles between the Wh and Gr parts of chimeric leaves using label-free LFQ intensity. In total, 855 succinylated sites in 335 proteins were identified, and 593 succinylated sites in 237 proteins were quantified. Compared to the Gr parts, 232 (61.1%) sites in 128 proteins were quantified as upregulated targets, and 148 (38.9%) sites in 70 proteins were quantified as downregulated targets in the Wh parts of chimeric leaves using a 1.5-fold threshold (P < 0.05). These proteins with altered succinylation level were mainly involved in crassulacean acid metabolism (CAM) photosynthesis, photorespiration, glycolysis, the citric acid cycle (CAC) and pyruvate metabolism. Our results suggested that the changed succinylation level in proteins might function in the main energy metabolism pathways-photosynthesis and respiration. Succinylation might provide a significant effect in the growth of chimeric leaves and the relationship between the Wh and Gr parts of chimeric leaves. This study not only provided a basis for further characterization on the function of succinylated proteins in chimeric leaves of Ananas comosus var. bracteatus but also provided a new insight into molecular breeding for leaf color chimera.
Editor: England: BioMed Central Ltd
Idioma: Inglês

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Systematic identification and comparative analysis of lysine succinylation between the green and white parts of chimeric leaves of Ananas comosus var. bracteatus

Mao, Meiqin ; Xue, Yanbin ; He, Yehua ; Zhou, Xuzixing ; Rafique, Fatima ; Hu, Hao ; Liu, Jiawen ; Feng, Lijun ; Yang, Wei ; Li, Xi ; Sun, Lingxia ; Huang, Zhuo ; Ma, Jun

England: BioMed Central Ltd

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