Proteomics

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Identification and Analysis of Fha-Interacting Proteins in Vibrio cholerae

ABSTRACT: This study aimed to identify proteins interacting with Fha in Vibrio cholerae. A Strep-tagged Fha fusion protein (Fha-Strep) was expressed in Vibrio cholerae, and associated protein complexes were enriched using Strep-Tactin affinity purification following cell lysis. As a negative control, an sfGFP-Strep fusion protein was expressed and processed in parallel. The enriched protein samples were subjected to tryptic digestion and analyzed by liquid chromatography–tandem mass spectrometry (LC-MS/MS) using a timsTOF Pro mass spectrometer operated in dia-PASEF mode. This approach enabled comprehensive identification and quantification of Fha-associated proteins. Three biological replicates were included for each group to ensure reproducibility. The resulting dataset provides a resource for understanding the interaction network of Fha and its potential role in the Type VI Secretion System (T6SS) in Vibrio cholerae.

ORGANISM(S): Vibrio Cholerae O1 Biovar El Tor Str. N16961

SUBMITTER: Tao Dong  

PROVIDER: PXD078046 | iProX | Fri May 01 00:00:00 BST 2026

REPOSITORIES: iProX

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Gene-in-gene coding generates dual-isoform Fha condensates to control type VI secretion system assembly.

Pei Tong-Tong TT   Chen Qiao-Yu QY   Wang Xing-Yu XY   Ma Amy A   Liang Jia-Xin JX   Ye Zi-Yan ZY   Liu Yu-Zhao YZ   Su Jing-Tong JT   Liang Xiaoye X   An Ying Y   Zhu Jun J   Dong Tao T  

Nature communications 20260526

While eukaryotes employ alternative splicing to diversify protein functions, analogous strategies in bacteria remain underexplored. Here we identify a conserved intragenic coding mechanism in Vibrio cholerae that generates two isoforms of the essential scaffold Fha and show that these isoforms cooperate through liquid-liquid phase separation to promote the assembly of the type VI secretion system (T6SS). The full-length isoform, Fha<sup>L</sup>, seeds assembly by engaging the membrane complex, w  ...[more]

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