PXD057351

PXD057351 is an original dataset announced via ProteomeXchange.

Title	PII interactions with the acetyl-CoA carboxylase subunits BADC and BCCP co-regulate lipid and nitrogen metabolism in Arabidopsis
Description	In plants the initiation of fatty acid synthesis is catalyzed by acetyl-CoA carboxylase (ACCase) which produces malonyl-CoA. The heteromeric form of ACCase (htACCase) is a holoenzyme consisting of biotin carboxylase and carboxyltransferase sub-complexes, both of which are subject to extensive regulation. Biotin carboxylase activity is controlled in part by the presence of the catalytic biotin carboxyl carrier proteins (BCCP1/2) and/or the non-catalytic, non-biotinylated, biotin/lipoyl attachment domain-containing proteins (BADC1/2/3) that associate with backbone biotin carboxylase (BC) protein. However, the mechanisms regulating BADC and BCCP interaction with BC and thus ACCase activity in planta are not clear. Here we demonstrate the Arabidopsis thaliana regulatory protein PII modulates htACCase activity through independent interactions with BADC and BCCP proteins in a selective manner. Analysis of badc1/2 and badc1/3 mutant lines and the respective pii triple mutants reveal that changes in seed oil and protein accumulation of badc double mutants are PII/nitrogen dependent. Absolute quantification of htACCase subunits and PII in developing seeds suggests that Arabidopsis exerts tight regulation over individual protein stoichiometry to balance oil and protein accumulation. The effects on vegetative and seed development indicate PII and BADC proteins have distinct but overlapping roles in the regulation of plant metabolism.
HostingRepository	PRIDE
AnnounceDate	2025-12-16
AnnouncementXML	Submission_2025-12-16_07:21:07.893.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Gabriel Lemes Jorge
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: NEWT:3702;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	TSQ Altis Plus

Revision	Datetime	Status	ChangeLog Entry
0	2024-10-30 06:12:51	ID requested
⏵ 1	2025-12-16 07:21:08	announced

10.1093/PLPHYS/KIAF627;

submitter keyword: None

Philip D.
contact affiliation	Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164, United States
contact email	phil_bates@wsu.edu
lab head
Gabriel Lemes Jorge
contact affiliation	University of Missouri
contact email	glj2d5@umsystem.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/12/PXD057351

PRIDE project URI

• PRIDE
  1. PXD057351
     1. Label: PRIDE project
     2. Name: PII interactions with the acetyl-CoA carboxylase subunits BADC and BCCP co-regulate lipid and nitrogen metabolism in Arabidopsis