PXD063736

PXD063736 is an original dataset announced via ProteomeXchange.

Title	Identifying peptides and sites involved in FtsZ self-assembly in Escherichia coli through in vivo protein photocrosslinking of FtsZ residues mediated by the unnatural amino acid Bpa (p-benzoyl-L-phenylalanine), followed by tandem mass spectrometry analysis of purified FtsZ crosslinking dimers.
Description	Bacterial cell division hinges on the Z-ring, an architecture built from the dynamical assembly and disassembly of FtsZ proteins. This delicate balance ensures not only apparent stability, but also continuous remodeling, both of which are required for Z-ring functioning. However, the molecular nature of such subcellular structures remains elusive. In searching for elusive FtsZ self-assembly interfaces involved in assembling the dynamic Z-ring in bacterial cells, we performed in vivo protein photocrosslinking for FtsZ residues as mediated by the unnatural amino acid Bpa and found some N-IDR and N-domain residues were involved in FtsZ self-assembly interactions. To identify counterpart surfaces with which the N-IDR and N-domain interacted when FtsZ self-assembled, we characterized FtsZ peptides and residues that were crosslinked to Bpa residues introduced into these regions by performing tandem mass spectrometry on purified FtsZ crosslinking dimers. Surprisingly, we observed that Bpa residues introduced to the N-IDR (e.g., at T8 or D10) crosslinked with residues in the N-domain, while Bpa residues introduced to the N-domain (e.g., at F40, K51, Q56 or S62) crosslinked with residues in the N-IDR. These crosslinking results strongly suggested that the N-IDR of one subunit interacted with the N-domain of a neighbouring subunit and vice versa when FtsZ self-assembled in cells.
HostingRepository	PRIDE
AnnounceDate	2025-05-10
AnnouncementXML	Submission_2025-05-10_05:44:38.252.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Huijia Yin
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2025-05-07 10:33:29	ID requested
⏵ 1	2025-05-10 05:44:38	announced

Dataset with its publication pending

submitter keyword: Escherichia coli,FtsZ, bacterial cell division, p-benzoyl-l-phenylalanine, photocrosslinking

Zengyi Chang
contact affiliation	School of Life Sciences, Peking University, Beijing 100871, P.R. China
contact email	changzy@pku.edu.cn
lab head
Huijia Yin
contact affiliation	School of Life Sciences, Peking University, Beijing 100871, P.R. China
contact email	yihuji@126.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD063736
     1. Label: PRIDE project
     2. Name: Identifying peptides and sites involved in FtsZ self-assembly in Escherichia coli through in vivo protein photocrosslinking of FtsZ residues mediated by the unnatural amino acid Bpa (p-benzoyl-L-phenylalanine), followed by tandem mass spectrometry analysis of purified FtsZ crosslinking dimers.