Distinct TssA proteins converge in coordinating tail biogenesis of the type VI secretion systems-Reference-Cited by-同舟云学术

Distinct TssA proteins converge in coordinating tail biogenesis of the type VI secretion systems

Published:2022-11-20 Issue:2 Volume:45 Page:2200219
ISSN:0265-9247
Container-title:BioEssays
language:en
Short-container-title:BioEssays

Author:

Ali Jemal¹²³,Lai Erh‐Min¹²⁴^ORCID

Affiliation:

1. Institute of Plant and Microbial Biology Academia Sinica Taipei Taiwan

2. Molecular and Biological Agricultural Sciences Program Taiwan International Graduate Program National Chung‐Hsing University and Academia Sinica Taipei Taiwan

3. Graduate Institute of Biotechnology National Chung‐Hsing University Taichung Taiwan

4. Biotechnology Center National Chung‐Hsing University Taichung Taiwan

Publisher

Wiley

Subject

General Biochemistry, Genetics and Molecular Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bies.202200219

Reference6 articles.

1. Priming and polymerization of a bacterial contractile tail structure

2. TssA forms a gp6‐like ring attached to the type VI secretion sheath

3. TssA: The cap protein of the Type VI secretion system tail

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1. Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains;Nature Communications;2024-05-20

2. A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells;EMBO reports;2023-04-17

3. Sporulation Activated via σ ^W Protects Bacillus from a Tse1 Peptidoglycan Hydrolase Type VI Secretion System Effector;Microbiology Spectrum;2023-04-13

4. A glycine zipper motif governs translocation of type VI secretion toxic effectors across the cytoplasmic membrane of target cells;2022-07-13