Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia.
Alternative splicing
Dephosphorylation
Ethylene
Petunia
Phosphorylation
Senescence
Journal
BMC plant biology
ISSN: 1471-2229
Titre abrégé: BMC Plant Biol
Pays: England
ID NLM: 100967807
Informations de publication
Date de publication:
03 Nov 2021
03 Nov 2021
Historique:
received:
17
04
2021
accepted:
18
10
2021
entrez:
4
11
2021
pubmed:
5
11
2021
medline:
28
12
2021
Statut:
epublish
Résumé
Senescence represents the last stage of flower development. Phosphorylation is the key posttranslational modification that regulates protein functions, and kinases may be more required than phosphatases during plant growth and development. However, little is known about global phosphorylation changes during flower senescence. In this work, we quantitatively investigated the petunia phosphoproteome following ethylene or air treatment. In total, 2170 phosphosites in 1184 protein groups were identified, among which 2059 sites in 1124 proteins were quantified. To our surprise, treatment with ethylene resulted in 697 downregulated and only 117 upregulated phosphosites using a 1.5-fold threshold (FDR < 0.05), which showed that ethylene negatively regulates global phosphorylation levels and that phosphorylation of many proteins was not necessary during flower senescence. Phosphoproteome analysis showed that ethylene regulates ethylene and ABA signalling transduction pathways via phosphorylation levels. One of the major targets of ethylene-induced dephosphorylation is the plant mRNA splicing machinery, and ethylene treatment increases the number of alternative splicing events of precursor RNAs in petunia corollas. Protein dephosphorylation could play an important role in ethylene-induced senescence, and ethylene treatment increased the number of AS precursor RNAs in petunia corollas.
Sections du résumé
BACKGROUND
BACKGROUND
Senescence represents the last stage of flower development. Phosphorylation is the key posttranslational modification that regulates protein functions, and kinases may be more required than phosphatases during plant growth and development. However, little is known about global phosphorylation changes during flower senescence.
RESULTS
RESULTS
In this work, we quantitatively investigated the petunia phosphoproteome following ethylene or air treatment. In total, 2170 phosphosites in 1184 protein groups were identified, among which 2059 sites in 1124 proteins were quantified. To our surprise, treatment with ethylene resulted in 697 downregulated and only 117 upregulated phosphosites using a 1.5-fold threshold (FDR < 0.05), which showed that ethylene negatively regulates global phosphorylation levels and that phosphorylation of many proteins was not necessary during flower senescence. Phosphoproteome analysis showed that ethylene regulates ethylene and ABA signalling transduction pathways via phosphorylation levels. One of the major targets of ethylene-induced dephosphorylation is the plant mRNA splicing machinery, and ethylene treatment increases the number of alternative splicing events of precursor RNAs in petunia corollas.
CONCLUSIONS
CONCLUSIONS
Protein dephosphorylation could play an important role in ethylene-induced senescence, and ethylene treatment increased the number of AS precursor RNAs in petunia corollas.
Identifiants
pubmed: 34732145
doi: 10.1186/s12870-021-03286-x
pii: 10.1186/s12870-021-03286-x
pmc: PMC8565076
doi:
Substances chimiques
Ethylenes
0
Plant Proteins
0
Proteome
0
ethylene
91GW059KN7
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
512Informations de copyright
© 2021. The Author(s).
Références
Food Res Int. 2020 May;131:108975
pubmed: 32247445
Plant Physiol. 2005 Jun;138(2):1018-26
pubmed: 15894742
Plant Cell Physiol. 2011 Apr;52(4):651-62
pubmed: 21382977
Plant Cell. 2004 Dec;16(12):3386-99
pubmed: 15539472
Arch Biochem Biophys. 2004 Aug 1;428(1):81-91
pubmed: 15234272
Chromosoma. 2013 Jun;122(3):191-207
pubmed: 23525660
Nat Methods. 2015 Apr;12(4):357-60
pubmed: 25751142
Nat Methods. 2009 Nov;6(11):786-7
pubmed: 19876014
Plant Mol Biol. 2000 Oct;44(3):303-18
pubmed: 11199390
BMC Plant Biol. 2014 Nov 18;14:307
pubmed: 25403317
Gene. 2012 May 1;498(2):155-63
pubmed: 22548231
Plant Physiol. 2009 Jun;150(2):889-903
pubmed: 19376835
Plant Physiol. 1998 Feb 1;116(2):833-44
pubmed: 9490775
Front Plant Sci. 2015 Oct 21;6:879
pubmed: 26557127
Mol Biosyst. 2011 Sep;7(9):2637-50
pubmed: 21713283
J Biol Chem. 2007 Aug 24;282(34):25020-9
pubmed: 17586809
J Proteomics. 2013 Jan 14;78:486-98
pubmed: 23111157
Mol Plant. 2008 Mar;1(2):380-7
pubmed: 19825547
Hortic Res. 2015 Dec 16;2:15059
pubmed: 26715989
PLoS One. 2013 Jul 09;8(7):e65800
pubmed: 23874385
Plant Physiol. 2020 Aug;183(4):1710-1724
pubmed: 32461301
Plant Physiol. 1998 Jan;116(1):419-28
pubmed: 9449850
Plant Mol Biol. 2015 Jan;87(1-2):169-80
pubmed: 25425166
Mol Plant. 2014 Aug;7(8):1384-1387
pubmed: 24618881
Proc Natl Acad Sci U S A. 2001 Jan 2;98(1):373-8
pubmed: 11114160
BMC Plant Biol. 2005 Aug 10;5:14
pubmed: 16091151
Plant Cell. 2011 Mar;23(3):873-94
pubmed: 21447789
J Am Heart Assoc. 2013 Aug 07;2(4):e000318
pubmed: 23926118
Plant J. 2008 Apr;54(1):129-40
pubmed: 18182027
Plant Physiol. 2011 Dec;157(4):2131-53
pubmed: 22034630
J Biol Chem. 2004 Nov 19;279(47):48734-41
pubmed: 15358768
Plant Biotechnol J. 2020 Jan;18(1):287-297
pubmed: 31222853
J Proteome Res. 2015 May 1;14(5):2017-25
pubmed: 25751157
J Cell Sci. 2013 Nov 1;126(Pt 21):4823-33
pubmed: 24144694
Plant Physiol. 2012 Sep;160(1):488-97
pubmed: 22797658
Plant Physiol. 2009 May;150(1):167-77
pubmed: 19251906
Plant Physiol. 1999 Feb;119(2):755-64
pubmed: 9952472
Plant Physiol. 1993 Sep;103(1):31-9
pubmed: 7516081
F1000Res. 2013 Sep 16;2:188
pubmed: 24555089
Proc Natl Acad Sci U S A. 2012 Nov 20;109(47):19486-91
pubmed: 23132950
J Proteome Res. 2006 Nov;5(11):3084-95
pubmed: 17081060
Plant Physiol Biochem. 2018 Sep;130:173-180
pubmed: 29990770
J Exp Bot. 2008;59(8):2161-9
pubmed: 18535299
Plant Physiol. 2004 Oct;136(2):2900-12
pubmed: 15466231
Plant Mol Biol. 1993 Dec;23(6):1151-64
pubmed: 8292780
Hortic Res. 2016 Apr 27;3:16012
pubmed: 27162640
Elife. 2014 Jun 19;3:
pubmed: 24948515
Plant Cell Physiol. 2010 Nov;51(11):1821-39
pubmed: 20980270
Nat Protoc. 2016 Dec;11(12):2301-2319
pubmed: 27809316
J Exp Bot. 2010 Feb;61(4):1089-109
pubmed: 20110265
Mol Plant Microbe Interact. 2008 Oct;21(10):1275-84
pubmed: 18785823
Plant Signal Behav. 2019;14(10):e1642037
pubmed: 31314681
J Exp Bot. 2008;59(3):453-80
pubmed: 18310084
Mol Cell Proteomics. 2012 Nov;11(11):1140-55
pubmed: 22843990
Science. 1995 May 5;268(5211):667-75
pubmed: 7732375
Nucleic Acids Res. 2010 Jan;38(Database issue):D190-5
pubmed: 19900971
J Exp Bot. 2009;60(12):3311-36
pubmed: 19567479
J Proteomics. 2013 Nov 20;93:276-94
pubmed: 23435059
Front Plant Sci. 2016 Nov 01;7:1606
pubmed: 27847510
Plant Physiol. 1996 Oct;112(2):503-511
pubmed: 12226406
Plant J. 2012 Feb;69(4):667-78
pubmed: 22007837
J Integr Plant Biol. 2012 Aug;54(8):526-39
pubmed: 22709441
Trends Plant Sci. 2005 May;10(5):251-6
pubmed: 15882658
Plant Physiol. 2017 Jan;173(1):668-687
pubmed: 27810942
Phytochemistry. 2012 Dec;84:18-23
pubmed: 22989740
Plant Physiol. 2000 Jul;123(3):971-8
pubmed: 10889245
Annu Rev Plant Physiol Plant Mol Biol. 1996 Jun;47:101-125
pubmed: 15012284