Protein interactions within and between two F-type type IV secretion systems.

Mol Microbiol

Interdisciplinary Computing and Complex BioSystems (ICOS), School of Computing Science, Newcastle University, Newcastle upon Tyne, UK.

Published: November 2020

Bacterial type IV secretion systems (T4SSs) can mediate conjugation. The T4SS from Neisseria gonorrhoeae possesses the unique ability to mediate DNA secretion into the extracellular environment. The N. gonorrhoeae T4SS can be grouped with F-type conjugative T4SSs based on homology. We tested 17 proteins important for DNA secretion by N. gonorrhoeae for protein interactions. The BACTH-TM bacterial two-hybrid system was successfully used to study periplasmic interactions. By determining if the same interactions were observed for F-plasmid T4SS proteins and when one interaction partner was replaced by the corresponding protein from the other T4SS, we aimed to identify features associated with the unique function of the N. gonorrhoeae T4SS as well as generic features of F-type T4SSs. For both systems, we observed already described interactions shared by homologs from other T4SSs as well as new and described interactions between F-type T4SS-specific proteins. Furthermore, we demonstrate, for the first-time, interactions between proteins with homology to the conserved T4SS outer membrane core proteins and F-type-specific proteins and we confirmed two of them by co-purification. The F-type-specific protein TraH was found to localize to the outer membrane and the presence of significant amounts of TraH in the outer membrane requires TraG .

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8015186PMC
http://dx.doi.org/10.1111/mmi.14582DOI Listing

Publication Analysis

Top Keywords

outer membrane
12
protein interactions
8
interactions f-type
8
type secretion
8
secretion systems
8
dna secretion
8
gonorrhoeae t4ss
8
described interactions
8
t4ss
6
proteins
6

Similar Publications

Our current understanding of protein folding is based predominantly on studies of small (<150 aa) proteins that refold reversibly from a chemically denatured state. As protein length increases, the competition between off-pathway misfolding and on-pathway folding likewise increases, creating a more complex energy landscape. Little is known about how intermediates populated during the folding of larger proteins affect navigation of this more complex landscape.

View Article and Find Full Text PDF

Unlabelled: The complement cascade is a front-line defense against pathogens. Complement activation generates the membrane attack complex (MAC), a 10-11 nm diameter pore formed by complement proteins C5b through C8 and polymerized C9. The MAC embeds within the outer membrane of Gram-negative bacteria and displays bactericidal activity.

View Article and Find Full Text PDF

A OHCs-Targeted Strategy for PEDF Delivery in Noise-Induced Hearing Loss.

Adv Healthc Mater

January 2025

Department of Otorhinolaryngology-Head and Neck Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, 221002, P. R. China.

Noise-induced hearing loss (NIHL) results from prolonged exposure to intense noise, causing damage to sensory outer hair cells (OHCs) and spiral ganglion neurons (SGNs). The blood labyrinth barrier (BLB) hinders systemic drug delivery to the inner ear. This study applied a retro-auricular round window membrane (RWM) method to bypass the BLB, enabling the transport of macromolecular proteins into the inner ear.

View Article and Find Full Text PDF

Polymyxins are last-resort antimicrobial peptides administered clinically against multi-drug resistant bacteria, specifically in the case of Gram-negative species. However, an increasing number of these pathogens employ a defense strategy that involves a relay of enzymes encoded by the pmrE (ugd) loci and the arnBCDTEF operon. The pathway modifies the lipid-A component of the outer membrane (OM) lipopolysaccharide (LPS) by adding a 4-amino-4-deoxy-l-arabinose (L-Ara4N) headgroup, which renders polymyxins ineffective.

View Article and Find Full Text PDF

Isolation, purification and identification of antibacterial peptides from Jinhua ham broth and molecular simulation analyses of their interaction with bacterial porins.

Food Chem

January 2025

Key Laboratory of Meat Processing and Quality Control, Ministry of Education China, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. Electronic address:

The bioactive peptides in Jinhua ham could be released into the broth during cooking. After comparing peptide antibacterial activity from Jinhua ham broth with varying cooking durations, the cooking-2-h broths were selected for further analysis using cation-exchange and reverse-phase-liquid chromatography. The purified peptide sequences were subsequently synthesized and tested for their antibacterial activity.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!