PXD009710

PXD009710 is an original dataset announced via ProteomeXchange.

Title	Proteomes of dissected developing barley endosperm layers and microscopy identifies the starchy endosperm as prominent tissue for the storage of ER derived hordeins accompanied by the accumulation of HvPDIL1-1 and its intracellular re-localization
Description	Barley (Hordeum vulgare) is one of the major food sources for humans and forage source for animal livestock. Barley endosperm is structured into three distinct cell layers: the starchy endosperm, which acts essentially as storage tissue for starch, the subaleurone, which is characterized by a high accumulation of endoplasmic reticulum (ER)-derived seed storage proteins (SSP) and finally the aleurone beside the seed coat with a prominent role during seed germination. Prolamins account for more than 50% of the total protein amount in mature seeds. Together with other seed storage proteins (SSPs) they are important for both grain quality and flour quality. Prolamins are synthesized on the rough ER, translocated into the ER lumen and accumulate in distinct, ER-derived protein bodies (PBs) that are most abundant in the SE. PB formation is regulated by the protein disulfide isomerase (PDI) that is involved in the disulfide transfer pathway. Here, we used laser microdisection (LMD) to characterize spatio-temporal molecular and morphological differences of the ER during barley endosperm development. We revealed by nanoLC-MS/MS proteomic analyses performed on whole seeds and collected tissues at different seed development stages that the protein level of the protein disulfide isomerase HvPDIL1-1 is spatio-temporally regulated in developing barley endosperm. Our microscopic studies showed that HvPDIL1-1 preferentially accumulates in SE, especially at 12 days after pollination (dap). HvPDIL1-1 re-localized from PBs to the protein matrix at the periphery of starch granules along grain filling process. Detailed analysis of SE proteome dynamics identified clusters of proteins with similar expression pattern as HvPDIL1-1, which were analysed in a protein-protein network. It revealed a strong functional interconnection between transcription and translation, protein folding and amino acid synthesis with sucrose and starch metabolism. Our data indicate a role of HvPDIL1-1 in the coordination of protein synthesis and prolamins deposition during grain filling processes in developing barley endosperm. These results are discussed in relation to the putative role of HvPDIL1-1 for cereal food end-product quality and recombinant protein production in cereal seeds.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:44:54.590.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Valentin Roustan
SpeciesList	scientific name: Hordeum vulgare (Barley); NCBI TaxID: 4513;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2018-05-08 04:35:53	ID requested
1	2018-10-01 08:38:01	announced
⏵ 2	2024-10-22 04:44:55	announced	2024-10-22: Updated project metadata.

Roustan V, Roustan PJ, Weidinger M, Reipert S, Kapusi E, Shabrangy A, Stoger E, Weckwerth W, Ibl V, Microscopic and Proteomic Analysis of Dissected Developing Barley Endosperm Layers Reveals the Starchy Endosperm as Prominent Storage Tissue for ER-Derived Hordeins Alongside the Accumulation of Barley Protein Disulfide Isomerase (HvPDIL1-1). Front Plant Sci, 9():1248(2018) [pubmed]

10.3389/fpls.2018.01248;

curator keyword: Biological

submitter keyword: HvPDIL 1-1, barley caryopsis, shotgun proteomics, hordeins, endoplasmic reticulum, Laser Microdissection

Verena Ibl
contact affiliation	Department of Ecogenomics and Systems Biology, University of Vienna, Althanstrasse 14, 1090 Vienna, Austria
contact email	verena.ibl@univie.ac.at
lab head
Valentin Roustan
contact affiliation	University of Vienna
contact email	valentin.roustan@univie.ac.at
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/2018/10/PXD009710

PRIDE project URI

• PRIDE
  1. PXD009710
     1. Label: PRIDE project
     2. Name: Proteomes of dissected developing barley endosperm layers and microscopy identifies the starchy endosperm as prominent tissue for the storage of ER derived hordeins accompanied by the accumulation of HvPDIL1-1 and its intracellular re-localization