Comparative phosphoproteomic analysis of blast resistant and susceptible rice cultivars in response to salicylic acid

Sun, Ranran; Qin, Shiwen; Zhang, Tong; Wang, Zhenzhong; Li, Huaping; Li, Yunfeng; Nie, Yanfang

doi:10.1186/s12870-019-2075-5

Table 1 SA-responsive rice phosphoproteins identified by MALDI-TOF/TOF MS

From: Comparative phosphoproteomic analysis of blast resistant and susceptible rice cultivars in response to salicylic acid

Protein Spot No.^a	Protein Name	Uniprot Accession No.	Molecular Mass (kDa)	Isoelectric Point	Pep. Count^b	Protein Score^c	Protein Score (C.I.%)^d	Relative fold changes^e
Protein Spot No.^a	Protein Name	Uniprot Accession No.	Molecular Mass (kDa)	Isoelectric Point	Pep. Count^b	Protein Score^c	Protein Score (C.I.%)^d	CO39	C101LAC
Photosynthesis
1	HAD-superfamily hydrolase, subfamily IA, variant 3 containing protein, expressed	Q10I42	34.1	8.4	11	560	100	NC	↓ 12 h 1.93 ± 0.01
5	Rubisco activase, chloroplast precursor, putative, expressed	H2KWJ8	39	5.4	19	761	100	↑ 12 h 4.06 ± 0.32	↑ 12 h 4.43 ± 0.53
20	Rubisco large subunit	POC511	26	7.0	12	452	100	↑ 12 h 1.83 ± 0.17	↑12 h 1.94 ± 0.14
27	Putative transketolase 1	Q5VNW1	69.4	5.4	22	521	100	↑ 24 h 1.53 ± 0.02	↑ 24 h 1.90 ± 0.02
34	Chloroplast 23 kDa polypeptide of photosystem II	B0FFP0	20	5.6	11	755	100	↓ 24 h 2.89 ± 0.01	NC
Defense-related protein
37	Putative cinnamoyl-CoA reductase	Q69U05	36	5.7	16	398	100	NC	↑24 h 1.63 ± 0.026
Antioxidative enzymes
15	GDP-mannose 3,5-epimerase 1	A3C4S4	43	5.8	23	702	100	↓12 h 2.36 ± 0.02	NC
33	L-ascorbate peroxidase 1	B7E6Z4	27.3	5.4	14	496	100	↓24 h 1.93 ± 0.01	↓24 h 1.83 ± 0.03
Molecular chaperone
23	Putative chaperonin 60 beta	Q9LWT6	64	5.6	23	560	100	↑ 24 h 3.71 ± 0.17	↑ 24 h 2.20 ± 0.01
Protein synthesis and degradation
4	ATP-dependent Clp protease proteolytic subunit	Q6H7I9	32	6.7	5	328	100	↑ 12 h 1.59 ± 0.04	↑12 h 1.63 ± 0.03
6	Alpha/beta hydrolase	Q710Q1	18	8.9	8	415	100	↓ 12 h 2.24 ± 0.07	↑ 12 h 3.01 ± 047
11	Probable glutamyl endopeptidase, chloroplastic	Q10MJ1	104.48	5.7	26	621	100	NC	↑ 12 h 1.75 ± 0.02
12	Probable glutamyl endopeptidase, chloroplastic	Q10MJ1	104.48	5.7	26	621	100	↑ 12 h 1.70 ± 0.01	↑ 12 h 2.08 ± 0.28
13	Probable glutamyl endopeptidase, chloroplastic	Q10MJ1	104.48	5.7	26	621	100	NC	↑ 12 h 2.08 ± 0.08
28	Eukaryotic initiation factor 4A-1	P35683	47.3	5.4	23	719	100	↓ 24 h 1.61 ± 0.02	↑ 24 h 1.78 ± 0.03
30	Elongation factor Tu	Q6ZI53	51	6.2	21	608	100	↓ 24 h 1.62 ± 0.09	NC
Carbohydrate metabolism
9	Phosphoglycerate mutase	Q5QMK7	61	5.4	18	386	100	NC	↓ 12 h 2.53 ± 0.38
17	Glyceraldehyde-3-phosphate dehydrogenase	A2XC18	47.5	6.2	16	652	100	↑12 h 2.67 ± 0.17	↓ 12 h 2.99 ± 0.02
18	Glyceraldehyde-3-phosphate dehydrogenase	A2XC18	47.5	6.2	16	652	100	↑12 h 2.19 ± 0.05	↓ 12 h 2.89 ± 0.02
24	Alpha 1,4-glucan phosphorylase	Q9ATK9	105	5.4	24	508	100	↑24 h 1.58 ± 0.04	NC
25	Alpha 1,4-glucan phosphorylase	Q9ATK9	105	5.4	24	508	100	↑24 h 2.47 ± 0.29	↑ 24 h 1.87 ± 0.03
31	Phosphoribulokinase	Q6Z8F4	44.9	5.7	15	830	100	↓ 24 h 15.98 ± 0.55	↑ 24 h 3.60 ± 0.42
32	Phosphoribulokinase	Q8GRU9	44.9	5.7	18	624	100	↓ 24 h 2.07 ± 0.01	↑ 24 h 2.25 ± 0.03
Amino acid metabolism
16	Aspartate aminotransferase	Q84V24	46	5.9	25	859	100	↓12 h 2.09 ± 0.03	NC
36	Cysteine synthase	Q2QLX5	43.8	8.8	18	479	100	NC	↑24 h 2.04 ± 0.05
Energy metabolism
21	ATP synthase epsilon chain, chloroplastic	P0C2Z3	15.3	5.0	9	559	100	NC	↓12 h 1.82 ± 0.02
Metabolism
7	Probable bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic	Q6Z234	59.2	5.6	18	306	100	↑ 12 h 1.62 ± 0.13 ↑ 24 h 2.74 ± 0.10	↑ 24 h 2.87 ± 0.08
8	Probable bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic	Q6Z234	59.2	5.6	18	306	100	↑12 h 2.21 ± 0.09	↓12 h 3.15 ± 0.15
29	Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplast, putative, expressed	Q6AVT2	55.8	7.0	31	844	100	↓ 24 h 1.68 ± 0.09	↑ 24 h 3.46 ± 0.09

^aSpot numbers are according to 2DE gels as shown in Fig. 1
^bNumber of unique peptides matched to mass peaks
^cMS and MS/MS combined score
^dC.I. % for the protein score rates the confidence level of the Protein Score
^eThe fold changes listed in the table were derived by comparison of relative protein intensity between SA-treated and control, which were calculated with PDQuest 8.0 software. The detailed information of relative protein intensity was listed in Additional file 1: Fig. S2. Only the proteins with changes ≥1.5-fold were listed. “NC” indicates the proteins with no significant changes (<1.5-fold). Differentially regulated phosphoproteins were marked by arrow, which indicates up-(↑) or down-regulated (↓) phosphoproteins in response to SA treatment. The number with no parentheses indicated the fold changes of differentially regulated phosphoproteins in 2DE gels

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ISSN: 1471-2229

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