PXD032265

PXD032265 is an original dataset announced via ProteomeXchange.

Title	Broad-range metalloprotease profiling in plants uncovers immunity provided by defence-related metalloenzyme
Description	Plants encode for >100 metalloproteases representing >19 different protein families. Tools to study this large and diverse class of proteases have not yet been introduced into plant science. Here, we used hydroxamate-based photoaffinity probes to explore plant proteomes for metalloproteases. We detected labeling of 23 metalloproteases in leaf extracts of the model plant Arabidopsis thaliana that belong to eight unrelated metalloprotease families and localize to different subcellular compartments. We identified several chloroplast localized FtsH proteases; vacuolar aspartyl aminopeptidase DAP1; peroxisomal metalloprotease PMX16; and many cytosolic metalloproteases. We also identified non-proteolytic metallohydrolases involved the release of auxin and in the urea cycle. Studies on tobacco plant Nicotiana benthamiana infected with the bacterial plant pathogen Pseudomonas syringae uncovered PRp27, a secreted protein with anticipated metalloprotease activity. PRp27 depletion increases susceptibility, whilst its overexpression increases resistance, dependent on the presence of active site residues. Collectively, these studies uncover the strength of hydroxamate-based probes to study metalloenzymes in plants
HostingRepository	PRIDE
AnnounceDate	2022-08-12
AnnouncementXML	Submission_2022-08-12_00:03:41.451.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Kyoko Morimto
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; scientific name: Nicotiana benthamiana; NCBI TaxID: 4100;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-03-14 09:41:41	ID requested
⏵ 1	2022-08-12 00:03:42	announced

Morimoto K, Krahn D, Kaschani F, Hopkinson-Woolley D, Gee A, Buscaill P, Mohammed S, Sieber SA, Cravatt BF, Schofield CJ, van der Hoorn RAL, Broad-range metalloprotease profiling in plants uncovers immunity provided by defence-related metalloenzyme. New Phytol, 235(3):1287-1301(2022) [pubmed]

submitter keyword: Arabidopsis, metalloproteases, photoaffinity labelling, PRp27, immunity

Renier A. L. van der Hoorn1
contact affiliation	The Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom
contact email	renier.vanderhoorn@plants.ox.ac.uk
lab head
Kyoko Morimto
contact affiliation	Kyomei
contact email	kyoko@kyomei.co.uk
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/2022/08/PXD032265

PRIDE project URI

• PRIDE
  1. PXD032265
     1. Label: PRIDE project
     2. Name: Broad-range metalloprotease profiling in plants uncovers immunity provided by defence-related metalloenzyme