PXD031886

PXD031886 is an original dataset announced via ProteomeXchange.

Title	Analysis of the extracellular proteome from Aspergillus nidulans growing in Avicel, sugarcane bagasse and sugarcane straw
Description	Lytic polysaccharide monooxygenases (LPMOs) are oxidative enzymes found in viruses, archaea, bacteria as well as eukaryotes, such as fungi, algae and insects, actively contributing to the degradation of different polysaccharides. Analysis of the extracellular proteome (secretome) from Aspergillus nidulans growing in Avicel, sugarcane bagasse and sugarcane straw and analysed by LC-MS/MS in a LTQ Orbitrap Velos revealed that up to five LPMOs from family AA9 (AnLPMO9s), along with an AA3 cellobiose dehydrogenase (AnCDH1), are co-secreted upon growth on crystalline cellulose and lignocellulosic substrates, indicating their role in the degradation of plant cell wall components. Functional analysis revealed that the three main secreted LPMO9s (AnLPMO9C, AnLPMO9F and AnLPMO9G) correspond to cellulose- active enzymes with distinct regioselectivity. Deletion and overexpression studies confirmed that the abundantly secreted AnLPMO9F is a major component of the extracellular cellulolytic system, while AnLPMO9G, less abundant in the secretome, and has an important role by oxidizing crystalline fractions of cellulose. Single or double deletion of these AnLPMO9s partially impair fungal growth on sugarcane straw but not on crystalline cellulose, demonstrating the importance of LPMO9s for the saprophytic fungal lifestyle in the degradation of complex lignocellulosic substrates. Although the deletion of AnCDH1 slightly reduced the cellulolytic activity, it did not affect fungal growth indicating the existence of other electron donors to LPMOs. Additionally, double or triple knockouts of these enzymes had no accumulative deleterious effect on the cellulolytic activity nor on fungal growth, regardless of the deleted gene. Overexpression of AnLPMO9s in a cellulose-induced secretome background confirmed the importance and applicability of AnLPMO9G to improve lignocellulose saccharification.
HostingRepository	PRIDE
AnnounceDate	2022-05-31
AnnouncementXML	Submission_2022-05-31_02:16:30.733.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Marcelo Rubio
SpeciesList	scientific name: Aspergillus nidulans FGSC A4; NCBI TaxID: 227321;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2022-02-24 10:28:07	ID requested
⏵ 1	2022-05-31 02:16:31	announced

Dataset with its publication pending

submitter keyword: LPMO, AA9, oxidative enzymes, fungal biology, carbohydrate metabolism, sugarcane lignocellulose

André Damásio
contact affiliation	Laboratory of Enzymology and Molecular Biology (LEBIMO), Institute of Biology, University of Campinas (UNICAMP)
contact email	adamasio@unicamp.br
lab head
Marcelo Rubio
contact affiliation	University of Campinas
contact email	marcelov.rubio@gmail.com
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/2022/05/PXD031886

PRIDE project URI

• PRIDE
  1. PXD031886
     1. Label: PRIDE project
     2. Name: Analysis of the extracellular proteome from Aspergillus nidulans growing in Avicel, sugarcane bagasse and sugarcane straw