PXD024020 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Intramolecular synergism and proteolytic control of bacteriophage endolysin PlySK1249 |
Description | Endolysins are peptidoglycan hydrolases produced at the end of the bacteriophage (phage) replication cycle to lyse the host cell. Gram-positive phages endolysins come in a variety of multi-modular forms that combine different catalytic domains and may have evolved to adapt to their bacterial hosts. However, the reason why phage can adopt endolysin with such complex multidomain architecture is for the moment not well understood. We used the Streptococcus dysgalactiae phage endolysin PlySK1249 as a model to study the implication of multi-domain architecture in phage-induced bacterial lysis and lysis regulation. The activity of the enzyme relied on a bacteriolytic amidase (Ami), a non-bacteriolytic L-Ala-D-Ala endopeptidase (CHAP) acting as a de-chaining enzyme and central LysM cell wall binding domain (CBD). Ami and CHAP synergized for peptidoglycan digestion and bacteriolysis in the native enzyme or when expressed individually and reunified in vitro. This cooperation could be modulated by bacterial cell wall-associated proteases, which specifically cleaved the two linkers connecting the different domains. While both catalytic domains were observed to act coordinately to optimize bacterial lysis, the CBD is expected to delay diffusion of the enzyme until proteolytic inactivation is achieved. As for certain autolysins, PlySK1249 cleavage by bacterial cell wall associated proteases might be an example of dual phage-bacterial regulation and mutual coevolution. |
HostingRepository | PRIDE |
AnnounceDate | 2021-04-16 |
AnnouncementXML | Submission_2021-04-15_21:41:42.892.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD024020 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Patrice Waridel |
SpeciesList | scientific name: Streptococcus dysgalactiae subsp. equisimilis SK1249; NCBI TaxID: 1000589; scientific name: Streptococcus agalactiae FSL S3-026; NCBI TaxID: 876138; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Velos; Orbitrap Fusion; Q Exactive Plus |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-02-05 03:42:21 | ID requested | |
1 | 2021-04-15 00:39:08 | announced | |
⏵ 2 | 2021-04-15 21:41:43 | announced | 2021-04-16: Updated project metadata. |
Publication List
10.1016/J.JBC.2021.100639; |
Oechslin F, Menzi C, Moreillon P, Resch G, The multidomain architecture of a bacteriophage endolysin enables intramolecular synergism and regulation of bacterial lysis. J Biol Chem, 296():100639(2021) [pubmed] |
Keyword List
submitter keyword: endolysin, proteolysis,Bacteriophage, LC-MS/MS |
Contact List
Frank Oechslin |
contact affiliation | Department of Fundamental Microbiology, University of Lausanne, 1015 Lausanne, Switzerland. |
contact email | Frank.Oechslin@gmail.com |
lab head | |
Patrice Waridel |
contact affiliation | University of Lausanne |
contact email | patrice.waridel@unil.ch |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD024020
- Label: PRIDE project
- Name: Intramolecular synergism and proteolytic control of bacteriophage endolysin PlySK1249