PXD012663

PXD012663 is an original dataset announced via ProteomeXchange.

Title	Unraveling the essential cellulosomal components of the (Pseudo)Bacteroides cellulosolvens by massive proteomic analysis
Description	Background (Pseudo)Bacteroides cellulosolvens is a cellulolytic bacterium producing the most extensive and intricate cellulosomal system known in nature. Recently, an elaborate architecture of B. cellulosolvens cellulosomal system was revealed from its genome sequence analysis, and first evidence on the interactions between its structural and enzymatic components were detected in vitro. Yet, the cellulolytic potential of the bacterium in carbohydrate deconstruction may reside only within complete high-molecular weight protein complexes, which are secreted from the bacterium. Results The current proteome-wide work reveals patterns of protein expression of various cellulosomal components, and explores the differential expression signature upon bacterial growth two carbon sources, either cellobiose or microcrystalline cellulose. Mass spectrometry analysis of the bacterial secretome fraction revealed the expression of 24 scaffoldin structural units and 166 dockerin-bearing enzymes, in addition to free enzymatic subunits. All these components comprise cell-free and cell-bound cellulosomes for more efficient carbohydrate degradation. Various glycoside hydrolase (GH) family memebers were represented among 102 carbohydrate-degrading enzymes, including the most abundant GH48 exoglucanase. Specific cellulosomal components were associatred with different carbon sources, in cellulosomal fractions of different molecular weights. Overall, microcrystalline cellulose-derived cellulosomes showed higher expression levels of the structural and enzymatic components, and exhibited the highest degradation activity on five different carbohydrates. The cellulosomal activity of B. cellulosolvens showed high degradation rates that are very promising in biotechnological terms and were compatible with the activity levels exhibited by C. thermocellum purified cellulosomes. Conclusions The current research demonstrates the involvement of key cellulosomal factors participating in the mechanism of carbohydrate degradation by B. cellulosolvens. The powerful ability of the bacterium to exhibit different degradation strategies of various carbon sourcesis revealed. Thus, a novel components reservoir of degradation machineries that may serve for subsequent cellulosomal research, as a pool for designing new cellulolytic cocktails for biotechnological purposes.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:53:38.846.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Meital Kupervaser
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	deaminated residue; monohydroxylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-02-11 02:41:59	ID requested
1	2019-11-12 18:28:08	announced
⏵ 2	2024-10-22 04:53:39	announced	2024-10-22: Updated project metadata.

Zhivin-Nissan O, Dassa B, Morag E, Kupervaser M, Levin Y, Bayer EA, reveals an extensive reservoir of novel catalytic enzymes. Biotechnol Biofuels, 12():115(2019) [pubmed]

10.1186/s13068-019-1447-2;

submitter keyword: Biotechnology

Cohesin

Dockerin

Cellulolytic bacteria

CBM

Cellulases

Enzymatic hydrolysis

Glycoside hydrolases

Scaffoldin

Edward A. Bayer
contact affiliation	Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel
contact email	ed.bayer@weizmann.ac.il
lab head
Meital Kupervaser
contact affiliation	Weizmann Institute of Science
contact email	meital.kupervaser@weizmann.ac.il
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/2019/11/PXD012663

PRIDE project URI

• PRIDE
  1. PXD012663
     1. Label: PRIDE project
     2. Name: Unraveling the essential cellulosomal components of the (Pseudo)Bacteroides cellulosolvens by massive proteomic analysis