PaACL silencing accelerates flower senescence and changes the proteome to maintain metabolic homeostasis in Petunia hybrida.
ATP-citrate lyase
Acetyl-CoA
acetylome
metabolic homeostasis
petunia
proteome
Journal
Journal of experimental botany
ISSN: 1460-2431
Titre abrégé: J Exp Bot
Pays: England
ID NLM: 9882906
Informations de publication
Date de publication:
06 08 2020
06 08 2020
Historique:
received:
16
01
2020
accepted:
25
04
2020
pubmed:
5
5
2020
medline:
15
5
2021
entrez:
5
5
2020
Statut:
ppublish
Résumé
Cytosolic acetyl-CoA is an intermediate of the synthesis of most secondary metabolites and the source of acetyl for protein acetylation. The formation of cytosolic acetyl-CoA from citrate is catalysed by ATP-citrate lyase (ACL). However, the function of ACL in global metabolite synthesis and global protein acetylation is not well known. Here, four genes, PaACLA1, PaACLA2, PaACLB1, and PaACLB2, which encode the ACLA and ACLB subunits of ACL in Petunia axillaris, were identified as the same sequences in Petunia hybrida 'Ultra'. Silencing of PaACLA1-A2 and PaACLB1-B2 led to abnormal leaf and flower development, reduced total anthocyanin content, and accelerated flower senescence in petunia 'Ultra'. Metabolome and acetylome analysis revealed that PaACLB1-B2 silencing increased the content of many downstream metabolites of acetyl-CoA metabolism and the levels of acetylation of many proteins in petunia corollas. Mechanistically, the metabolic stress induced by reduction of acetyl-CoA in PaACL-silenced petunia corollas caused global and specific changes in the transcriptome, the proteome, and the acetylome, with the effect of maintaining metabolic homeostasis. In addition, the global proteome and acetylome were negatively correlated under acetyl-CoA deficiency. Together, our results suggest that ACL acts as an important metabolic regulator that maintains metabolic homeostasis by promoting changes in the transcriptome, proteome. and acetylome.
Identifiants
pubmed: 32364241
pii: 5828595
doi: 10.1093/jxb/eraa208
pmc: PMC7475263
doi:
Substances chimiques
Proteome
0
Acetyl Coenzyme A
72-89-9
ATP Citrate (pro-S)-Lyase
EC 2.3.3.8
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4858-4876Commentaires et corrections
Type : ErratumIn
Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissions@oup.com.
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