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pmid:27625672

Proteomic Studies on the Effects of Lipo-Chitooligosaccharide and Thuricin 17 under Unstressed and Salt Stressed Conditions in Arabidopsis thaliana.

Sowmyalakshmi Subramanian · Alfred Souleimanov · Donald L Smith

Frontiers in plant science · 2016 doi:10.3389/fpls.2016.01314

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Experiment

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Data

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title
Proteomic Studies on the Effects of Lipo-Chitooligosaccharide and Thuricin 17 under Unstressed and Salt Stressed Conditions in Arabidopsis thaliana.
doi
10.3389/fpls.2016.01314
pmid
27625672
authors array · 3 items
[0]
Sowmyalakshmi Subramanian
[1]
Alfred Souleimanov
[2]
Donald L Smith
journal
Frontiers in plant science
year
2016
abstract
Plants, being sessile organisms, are exposed to widely varying environmental conditions throughout their life cycle. Compatible plant-microbe interactions favor plant growth and development, and help plants deal with these environmental challenges. Microorganisms produce a diverse range of elicitor molecules to establish symbiotic relationships with the plants they associate with, in a given ecological niche. Lipo-chitooligosaccharide (LCO) and Thuricin 17 (Th17) are two such compounds shown to positively influence plant growth of both legumes and non-legumes. Arabidopsis thaliana responded positively to treatment with the bacterial signal compounds LCO and Th17 in the presence of salt stress (up to 250 mM NaCl). Shotgun proteomics of unstressed and 250 mM NaCl stressed A. thaliana rosettes (7 days post stress) in combination with the LCO and Th17 revealed many known, putative, hypothetical, and unknown proteins. Overall, carbon and energy metabolic pathways were affected under both unstressed and salt stressed conditions when treated with these signals. PEP carboxylase, Rubisco-oxygenase large subunit, pyruvate kinase, and proteins of photosystems I and II were some of the noteworthy proteins enhanced by the signals, along with other stress related proteins. These findings suggest that the proteome of A. thaliana rosettes is altered by the bacterial signals tested, and more so under salt stress, thereby imparting a positive effect on plant growth under high salt stress. The roles of the identified proteins are discussed here in relation to salt stress adaptation, which, when translated to field grown crops can be a crucial component and of significant importance in agriculture and global food production. The mass spectrometry proteomics data have been deposited to the ProteomeXchange with identifier PXD004742.
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The treatment contrasts were then analyzed for fold-change after normalization, and Fisher’s Exact test was used to narrow down the up- and down-regulated proteins, to predict their probable functions at 24 h after signal compound treatment and 7 days after NaCl stress imposition.
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sections[14] "Protein Profiling" paragraph 2
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The treatment contrasts were then analyzed for fold-change after normalization, and Fisher’s Exact test was used to narrow down the up- and down-regulated proteins, to predict their probable functions at 24 h after signal compound treatment and 7 days after NaCl stress imposition.
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium1 via the PRIDE partner repository (Vizcaino et al., 2013) with the dataset identifier PXD004742.
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sections[11] "Data Analysis" paragraph 3
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium1 via the PRIDE partner repository (Vizcaino et al., 2013) with the dataset identifier PXD004742.
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The paper reports that LCO and Th17 affected carbon and energy metabolic pathways under unstressed and salt-stressed conditions. Statistical analysis used fold change and Fisher’s exact test after embedded normalization of spectral quantitative values; the proteomics data were deposited in ProteomeXchange via PRIDE under identifier PXD004742.
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Overall, carbon and energy metabolic pathways were affected under both unstressed and salt stressed conditions when treated with these signals.
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sections[11] "Data Analysis" paragraph 3
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Scaffold 4.0 was used for analyzing the proteomics data for fold change and Fisher exact test of the identified proteins after subjecting the quantitative value of the spectra to the embedded normalization.
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sections[11] "Data Analysis" paragraph 3
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium1 via the PRIDE partner repository (Vizcaino et al., 2013) with the dataset identifier PXD004742.
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The paper reports that LCO and Th17 affected carbon and energy metabolic pathways under unstressed and salt-stressed conditions. Statistical analysis used fold change and Fisher’s exact test after embedded normalization of spectral quantitative values; the proteomics data were deposited in ProteomeXchange via PRIDE under identifier PXD004742.
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Arabidopsis rosettes proteome in response to LCO and Th17 under salt stress- LC-MS/MS
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Total number of proteins identified at 99% protein probability and total spectra at 95% peptide probability, with two minimum peptides.
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Stressed at 250 mM NaCl
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[1]
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491
[3]
461
[4]
456
[5]
457
[6]
506
[7]
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[8]
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Grouping of proteins in A. thaliana rosettes, that was significant in contrasts based on fold change.
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Protein Profiling
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Grouping of proteins in A. thaliana rosettes, that was significant in contrasts based on fold change.
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Treatment contrasts A. thaliana
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Control vs. LCO
[2]
Control vs. Th17
[3]
LCO vs. Th17
[4]
Control 250 mM NaCl vs. LCO + 250 mM NaCl
[5]
Control 250 mM NaCl vs. Th17 + 250 mM NaCl
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LCO 250 mM NaCl vs. Th17 + 250 mM NaCl
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[0]
Total significant proteins
[1]
114
[2]
93
[3]
80
[4]
93
[5]
92
[6]
80
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Known proteins
[1]
97
[2]
80
[3]
68
[4]
72
[5]
80
[6]
64
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8
[3]
8
[4]
13
[5]
15
[6]
11
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1
[3]
2
[4]
1
[5]
-
[6]
1
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4
[3]
2
[4]
7
[5]
7
[6]
4
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Grouping of proteins in A. thaliana rosettes, that were significant in contrasts based on Fisher’s Exact test.
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pmcid
PMC5003918
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Protein Profiling
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Table 3B
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Grouping of proteins in A. thaliana rosettes, that were significant in contrasts based on Fisher’s Exact test.
rows array · 6 items
[0] array · 7 items
[0]
Treatment contrasts A. thaliana
[1]
Control vs. LCO
[2]
Control vs. Th17
[3]
LCO vs. Th17
[4]
Control 250 mM NaCl vs. LCO + 250 mM NaCl
[5]
Control 250 mM NaCl vs. Th17 + 250 mM NaCl
[6]
LCO 250 mM NaCl vs. Th17 + 250 mM NaCl
[1] array · 7 items
[0]
Total significant proteins
[1]
63
[2]
42
[3]
26
[4]
25
[5]
40
[6]
25
[2] array · 7 items
[0]
Known proteins
[1]
55
[2]
33
[3]
22
[4]
21
[5]
34
[6]
20
[3] array · 7 items
[0]
Putative Proteins
[1]
7
[2]
8
[3]
2
[4]
4
[5]
5
[6]
5
[4] array · 7 items
[0]
Hypothetical proteins
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[2]
1
[3]
1
[4]
-
[5]
-
[6]
-
[5] array · 7 items
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[4]
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[5]
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Enzyme code distribution in un-stressed and salt stressed groups.
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Protein Profiling
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Enzyme code distribution in un-stressed and salt stressed groups.
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[0] array · 7 items
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Main enzyme classes
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[2]
LCOA
[3]
THA
[4]
250 mM NaCl Control
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LCOA + 250 mM NaCl
[6]
THA + 250 mM NaCl
[1] array · 7 items
[0]
Oxidoreductases
[1]
204
[2]
191 (↓6.58%)
[3]
197 (↓3.49%)
[4]
242
[5]
248 (↑2.45%)
[6]
269 (↑10.57%)
[2] array · 7 items
[0]
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[1]
91
[2]
157 (↑53.22%)
[3]
161 (↑55.55%)
[4]
170
[5]
169 (↓0.59%)
[6]
203 (↑17.7%)
[3] array · 7 items
[0]
Hydrolases
[1]
107
[2]
129 (↑ 18.64%)
[3]
136 (↑23.87%)
[4]
153
[5]
140 (↓8.87%)
[6]
166 (↑8.15%)
[4] array · 7 items
[0]
Lyases
[1]
40
[2]
63 (↑44.66%)
[3]
73 (↑58.40%)
[4]
69
[5]
72 (↑4.25%)
[6]
76 (↑9.65%)
[5] array · 7 items
[0]
Isomerases
[1]
51
[2]
42 (↓19.35%)
[3]
36 (↓34.48%)
[4]
47
[5]
36 (↓26.50%)
[6]
40 (↓16.09%)
[6] array · 7 items
[0]
Ligases
[1]
24
[2]
52 (↑73.68%)
[3]
51 (↑72%)
[4]
60
[5]
56 (↓6.89%)
[6]
65 (↑8%)
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Least square means of Arabidopsis thaliana percentage germination – seeds treated with lipo-chitooligosaccharide and Thuricin 17 under optimal conditions.
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A. thaliana Seed Germination in Petri Plates and Trays under Unstressed Conditions and in the Presence of Salt Stress Screening, When Treated with LCO and Th17
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Least square means of Arabidopsis thaliana percentage germination – seeds treated with lipo-chitooligosaccharide and Thuricin 17 under optimal conditions.
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75.52a
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1.04
[7]
87.83a
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1.11
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LCOB
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0.70
[5]
72.99a
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1.28
[7]
83.96a
[8]
1.57
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THA
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[3]
62.66a
[4]
0.53
[5]
78.87a
[6]
0.77
[7]
87.12a
[8]
0.76
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THB
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[3]
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[4]
0.97
[5]
75.81a
[6]
1.10
[7]
86.67a
[8]
1.12
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Total number of proteins identified at 99% protein probability and total spectra at 95% peptide probability, with two minimum peptides.
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Protein Profiling
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Table 2
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Total number of proteins identified at 99% protein probability and total spectra at 95% peptide probability, with two minimum peptides.
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Unstressed
[1]
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LCO 1
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457
[9]
464
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[7]
5902
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6009
[9]
5717
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Stressed at 250 mM NaCl
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[0]
Proteins
[1]
467
[2]
491
[3]
461
[4]
456
[5]
457
[6]
506
[7]
513
[8]
514
[9]
523
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[0]
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[1]
4753
[2]
5125
[3]
4945
[4]
4992
[5]
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5327
[7]
5336
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note
Grouping of proteins in A. thaliana rosettes, that was significant in contrasts based on fold change.
structure object · 5 fields
pmcid
PMC5003918
section_index
14
section_title
Protein Profiling
row_count
6
column_count
7
table object · 8 fields
label
Table 3A
caption
Grouping of proteins in A. thaliana rosettes, that was significant in contrasts based on fold change.
rows array · 6 items
[0] array · 7 items
[0]
Treatment contrasts A. thaliana
[1]
Control vs. LCO
[2]
Control vs. Th17
[3]
LCO vs. Th17
[4]
Control 250 mM NaCl vs. LCO + 250 mM NaCl
[5]
Control 250 mM NaCl vs. Th17 + 250 mM NaCl
[6]
LCO 250 mM NaCl vs. Th17 + 250 mM NaCl
[1] array · 7 items
[0]
Total significant proteins
[1]
114
[2]
93
[3]
80
[4]
93
[5]
92
[6]
80
[2] array · 7 items
[0]
Known proteins
[1]
97
[2]
80
[3]
68
[4]
72
[5]
80
[6]
64
[3] array · 7 items
[0]
Putative proteins
[1]
10
[2]
8
[3]
8
[4]
13
[5]
15
[6]
11
[4] array · 7 items
[0]
Hypothetical proteins
[1]
3
[2]
1
[3]
2
[4]
1
[5]
-
[6]
1
[5] array · 7 items
[0]
Unknown proteins
[1]
4
[2]
4
[3]
2
[4]
7
[5]
7
[6]
4
locator
section[14]/table-wrap[2]#T3a
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version
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note
Grouping of proteins in A. thaliana rosettes, that were significant in contrasts based on Fisher’s Exact test.
structure object · 5 fields
pmcid
PMC5003918
section_index
14
section_title
Protein Profiling
row_count
6
column_count
7
table object · 8 fields
label
Table 3B
caption
Grouping of proteins in A. thaliana rosettes, that were significant in contrasts based on Fisher’s Exact test.
rows array · 6 items
[0] array · 7 items
[0]
Treatment contrasts A. thaliana
[1]
Control vs. LCO
[2]
Control vs. Th17
[3]
LCO vs. Th17
[4]
Control 250 mM NaCl vs. LCO + 250 mM NaCl
[5]
Control 250 mM NaCl vs. Th17 + 250 mM NaCl
[6]
LCO 250 mM NaCl vs. Th17 + 250 mM NaCl
[1] array · 7 items
[0]
Total significant proteins
[1]
63
[2]
42
[3]
26
[4]
25
[5]
40
[6]
25
[2] array · 7 items
[0]
Known proteins
[1]
55
[2]
33
[3]
22
[4]
21
[5]
34
[6]
20
[3] array · 7 items
[0]
Putative Proteins
[1]
7
[2]
8
[3]
2
[4]
4
[5]
5
[6]
5
[4] array · 7 items
[0]
Hypothetical proteins
[1]
1
[2]
1
[3]
1
[4]
-
[5]
-
[6]
-
[5] array · 7 items
[0]
Unknown proteins
[1]
-
[2]
-
[3]
1
[4]
-
[5]
1
[6]
-
locator
section[14]/table-wrap[3]#T3b
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section[14]/table-wrap[4]#T4
version
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note
Enzyme code distribution in un-stressed and salt stressed groups.
structure object · 5 fields
pmcid
PMC5003918
section_index
14
section_title
Protein Profiling
row_count
7
column_count
7
table object · 8 fields
label
Table 4
caption
Enzyme code distribution in un-stressed and salt stressed groups.
rows array · 7 items
[0] array · 7 items
[0]
Main enzyme classes
[1]
Control
[2]
LCOA
[3]
THA
[4]
250 mM NaCl Control
[5]
LCOA + 250 mM NaCl
[6]
THA + 250 mM NaCl
[1] array · 7 items
[0]
Oxidoreductases
[1]
204
[2]
191 (↓6.58%)
[3]
197 (↓3.49%)
[4]
242
[5]
248 (↑2.45%)
[6]
269 (↑10.57%)
[2] array · 7 items
[0]
Transferases
[1]
91
[2]
157 (↑53.22%)
[3]
161 (↑55.55%)
[4]
170
[5]
169 (↓0.59%)
[6]
203 (↑17.7%)
[3] array · 7 items
[0]
Hydrolases
[1]
107
[2]
129 (↑ 18.64%)
[3]
136 (↑23.87%)
[4]
153
[5]
140 (↓8.87%)
[6]
166 (↑8.15%)
[4] array · 7 items
[0]
Lyases
[1]
40
[2]
63 (↑44.66%)
[3]
73 (↑58.40%)
[4]
69
[5]
72 (↑4.25%)
[6]
76 (↑9.65%)
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[0]
Isomerases
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51
[2]
42 (↓19.35%)
[3]
36 (↓34.48%)
[4]
47
[5]
36 (↓26.50%)
[6]
40 (↓16.09%)
[6] array · 7 items
[0]
Ligases
[1]
24
[2]
52 (↑73.68%)
[3]
51 (↑72%)
[4]
60
[5]
56 (↓6.89%)
[6]
65 (↑8%)
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section[14]/table-wrap[4]#T4
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asset:data:geo:PXD004742 not downloaded
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contingency_analysis
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chi_square_test
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quote
The treatment contrasts were then analyzed for fold-change after normalization, and Fisher’s Exact test was used to narrow down the up- and down-regulated proteins, to predict their probable functions at 24 h after signal compound treatment and 7 days after NaCl stress imposition.
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complete
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Computational analysis platform
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meta_analysis
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Automated Assays Laravel application and simulated adapters
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capability:computational_analysis
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The computational analysis is owned. The physical bench the paper used is not, so a physical validation cannot be run here.
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PXD004742
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PXD004742
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium1 via the PRIDE partner repository (Vizcaino et al., 2013) with the dataset identifier PXD004742.
basis
The paper names PXD004742 in ProteomeXchange Consortium via the PRIDE partner repository and the accession resolves in the repository. No dataset was downloaded and no licence was read.
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Compatible plant-microbe interactions favor plant growth and development, and help plants deal with these environmental challenges. Microorganisms produce a diverse range of elicitor molecules to establish symbiotic relationships with the plants they associate with, in a given ecological niche. Lipo-chitooligosaccharide (LCO) and Thuricin 17 (Th17) are two such compounds shown to positively influence plant growth of both legumes and non-legumes. Arabidopsis thaliana responded positively to treatment with the bacterial signal compounds LCO and Th17 in the presence of salt stress (up to 250 mM NaCl). Shotgun proteomics of unstressed and 250 mM NaCl stressed A. thaliana rosettes (7 days post stress) in combination with the LCO and Th17 revealed many known, putative, hypothetical, and unknown proteins. Overall, carbon and energy metabolic pathways were affected under both unstressed and salt stressed conditions when treated with these signals. PEP carboxylase, Rubisco-oxygenase large subunit, pyruvate kinase, and proteins of photosystems I and II were some of the noteworthy proteins enhanced by the signals, along with other stress related proteins. These findings suggest that the proteome of A. thaliana rosettes is altered by the bacterial signals tested, and more so under salt stress, thereby imparting a positive effect on plant growth under high salt stress. The roles of the identified proteins are discussed here in relation to salt stress adaptation, which, when translated to field grown crops can be a crucial component and of significant importance in agriculture and global food production. 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