PXD037937

PXD037937 is an original dataset announced via ProteomeXchange.

Title	The effect of multiple phaJ deletions Pseudomonas putida KT2440 on polyhydroxyalkanoates synthesis (part2)
Description	Pseudomonas putida KT2440 is a well-known model organism for the medium chain length (mcl) PHA accumulation. (R)-Specific enoyl-coenzyme A hydratase (PhaJ) was considered to be the main supplier of monomers for PHA synthesis by converting the -oxidation intermediate, trans-2-enoyl-CoA to (R)-3-hydroxyacyl-CoA when fatty acids (FA) are used. Three PhaJ homologues, PhaJ1, PhaJ4 and MaoC are annotated in P. putida KT2440. To investigate the relationship of fatty acids - PHA metabolism and the role of each PhaJ in PHA biosynthesis in P. putida KT2440, a series of P. putida KT2440 knockouts was obtained. PHA content and monomer composition in WT and mutants under different growth conditions were analysed. However, when all three PhaJ homologues were deleted, the mutant still accumulated PHA up to 10.7 % of the cell dry weight (CDW). To identify other potential PHA monomer suppliers by analysing the proteome of the phaJ1maoCphaJ4. The deletion of (R)-3-hydroxydecanoyl-ACP:CoA transacylase (PhaG), which connects de novo FA and PHA synthesis pathways, while causing further 1.8-fold decrease in PHA content, did not abolish PHA accumulation. Further proteome analysis revealed quinoprotein alcohol dehydrogeanses PedE and PedH as potential monomer suppliers, but when these were deleted PHA level remained at 2.2 – 14.8 % CDW depending on the fatty acid used, and whether nitrogen limitation was applied. To identify the other non-specific dehydrogenases supply monomers for PHA synthesis, we analysed the proteome of the sextuple mutant under nitrogen limiting and non-limiting conditions.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:47:24.295.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Si Liu
SpeciesList	scientific name: Pseudomonas putida KT2440; NCBI TaxID: 160488;
ModificationList	monohydroxylated residue
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2022-11-03 05:10:34	ID requested
1	2023-05-10 14:20:44	announced
⏵ 2	2023-11-14 08:47:32	announced	2023-11-14: Updated project metadata.

Liu S, Narancic T, Tham JL, O'Connor KE, -oxidation-polyhydroxyalkanoates synthesis relationship in Pseudomonas putida KT2440 revisited. Appl Microbiol Biotechnol, 107(5-6):1863-1874(2023) [pubmed]

submitter keyword: -oxidation pathway,Pseudomonas putida, polyhydroxyalkanoate, enzyme redundancy, de novo fatty acid synthesis

Kevin E. O’Connor
contact affiliation	UCD Earth Institute and School of Biomolecular and Biomedical Science, University College Dublin, Belfield, Dublin 4, Ireland BiOrbic - Bioeconomy Research centre, Ireland, University College Dublin, Belfield, Dublin 4, Ireland
contact email	kevin.oconnor@ucd.ie
lab head
Si Liu
contact affiliation	UCD School of Biomolecular and Biomedical Science
contact email	si.liu@ucd.ie
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD037937
     1. Label: PRIDE project
     2. Name: The effect of multiple phaJ deletions Pseudomonas putida KT2440 on polyhydroxyalkanoates synthesis (part2)