PXD042464-1

PXD042464 is an original dataset announced via ProteomeXchange.

Title	DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus
Description	Proteins containing a catalytically inactive LytM-type endopeptidase domain are important regulators of cell wall-degrading enzymes in bacteria. Here, we study their representative DipM, a factor mediating proper cell division in Caulobacter crescentus. We show that the LytM domain of DipM interacts with mul-tiple autolysins, including the lytic transglycosylases SdpA and SdpB, the amidase AmiC and the putative carboxypeptidase CrbA, and stimulates the activities of SdpA and AmiC. Its crystal structure displays a conserved groove, which is predicted to represent the dock¬ing site for autolysins by model¬ing studies. Mutations in this groove indeed abolish the function of DipM in vivo and its interaction with AmiC and SdpA in vitro. Notably, DipM and its regulatory targets SdpA and SdpB stimulate each other’s recruitment to the division site, establishing a self-reinforcing cycle that gradually increases autolytic activity as cyto¬kinesis progresses. DipM thus acts at the intersection of different peptidoglycan-remodeling pathways and coordinates their activities to ensure proper cell constriction and daughter cell separation.
HostingRepository	PRIDE
AnnounceDate	2023-05-24
AnnouncementXML	Submission_2023-05-24_00:53:07.559.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	TimoGlatter
SpeciesList	scientific name: Opecarcinus crescentus; NCBI TaxID: 2790513;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2023-05-24 00:42:50	ID requested
⏵ 1	2023-05-24 00:53:07	announced

Dataset with its publication pending

submitter keyword: autolysin, amidase, lytic transglycosylase, bacterial cell division, peptidoglycan,Bacteria, cell wall

TimoGlatter
contact affiliation	Max Planck Insitute for Terrestrial Microbiology Karl-von-Frisch Str. 10 35043 Marburg Germany
contact email	glatter@mpi-marburg.mpg.de
lab head
TimoGlatter
contact affiliation	MPI Marburg
contact email	glatter@mpi-marburg.mpg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD042464
     1. Label: PRIDE project
     2. Name: DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus