Edwardsiella tarda is a serious aquaculture pathogen that can infect many cultured fish species. The aim of this study was to investigate the potential importance of DNA adenine methylase (Dam) in E. tarda pathogenesis. The E. tarda dam gene (dam(Et)) was cloned from a pathogenic strain, TXD1, isolated from diseased fish. Dam(Et) shares high (70.2%) sequence identity with the Dam proteins of Yersinia enterocolitica and several other bacterial species. Recombinant Dam(Et) is able to complement a dam-deficient Escherichia coli strain and methylate the genomic DNA. Attenuation of dam(Et) expression by antisense RNA interference had no apparent effect on the growth of TXD1, but caused significant attenuation of overall bacterial virulence and altered several stress responses including spontaneous mutation, recovering from UV radiation and H(2)O(2) exposure, binding to host mucus, and dissemination in host blood and liver. In addition, attenuation of dam(Et) expression increased luxS expression and AI-2 activities in E. tarda. These results indicate that Dam(Et) is a virulence determinant and plays a role in the pathogenesis of TXD1, and that temporal expression of dam(Et) is essential for optimal bacterial infection.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.vetmic.2009.09.004 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Targeted DamID detects cell-type-specific histone modifications in intact tissues or organisms.
PLoS Biol
March 2025
The Gurdon Institute, University of Cambridge, Cambridge, United Kingdom.
Histone modifications play a key role in regulating gene expression and cell fate during development and disease. Current methods for cell-type-specific genome-wide profiling of histone modifications require dissociation and isolation of cells and are not compatible with all tissue types. Here we adapt Targeted DamID (TaDa) to recognize specific histone marks, by fusing chromatin-binding proteins or single-chain antibodies to Dam, an Escherichia coli DNA adenine methylase.
View Article and Find Full Text PDFTET2 suppresses vascular calcification by forming inhibitory complex with HDAC1/2 and SNIP1 independent of demethylation.
J Clin Invest
March 2025
Department of Cardiology, The Eighth Affiliated Hospital of Sun Yat-sen University, Shenzhen, China.
Osteogenic transdifferentiation of vascular smooth muscle cells (VSMCs) has been recognized as the principal mechanism underlying vascular calcification (VC). Runt-related transcription factor 2 (RUNX2) in VSMCs plays a pivotal role because it constitutes an essential osteogenic transcription factor for bone formation. As a key DNA demethylation enzyme, ten-eleven translocation 2 (TET2) is crucial in maintaining the VSMC phenotype.
View Article and Find Full Text PDFThe DNA N6-adenine methylation target gene GhMAF1 promotes fiber initiation at the base of Gossypium ovules.
New Phytol
March 2025
National Nanfan Research Institute (Sanya), Chinese Academy of Agricultural Sciences, Sanya, 572024, China.
DNA methylation consists of 5-methylcytosine and N6-methyl deoxyadenosine (6mA) and is crucial in plant development. However, its specific role and potential mechanism to initiate cotton fibers remain unclear. This study employed Oxford Nanopore Technologies (ONT) sequencing to analyze DNA methylation alterations in ZM24 and ZM24 fuzzless-lintless (ZM24fl) during fiber initiation.
View Article and Find Full Text PDFStudy of the DNA structure and orientation using SERS: Influence of the hybridisation and mismatches.
Int J Biol Macromol
March 2025
Institut des Molécules et Matériaux du Mans (IMMM UMR 6283 CNRS), Le Mans Université, Avenue Olivier Messiaen, CEDEX 9, 72085 Le Mans, France; Department of Laboratory Medicine, Southwest Hospital, Army Medical University (Third Military Medical University), Chongqing 400038, China; Nanobiophotonics and Laser Microspectroscopy Center, Interdisciplinary Research Institute in Bio-Nano-Sciences, Babes-Bolyai University, Cluj-Napoca, Romania. Electronic address:
In this article we study the structure and the orientation of DNA strands by Surface Enhanced Raman Scattering (SERS). We study the influence of two parameters on the structure of strands containing 20 adenines: the hybridization with the complementary strand and the presence of mismatch within the sequence. By varying the concentration of complementary strands, we show that hybridisation induces a change in strand orientation and loss of flexibility, indicating that the formation of the double helix freezes the conformation of DNA strand.
View Article and Find Full Text PDFAccurately sensing analysis of active adenine DNA glycosylase (MutY) via the high identification/excision capability to specific base-mismatches of dsDNA chains.
Int J Biol Macromol
March 2025
Research Center for Analytical Sciences, Department of Chemistry, College of Sciences, Northeastern University, Box 332, Shenyang 110819, China. Electronic address:
Adenine DNA glycosylase (MutY) is a crucial member of DNA glycosylase family, and the abnormal expression of the human MutY homologs is associated with the pathogenesis of various diseases, therefore, convenient and cost-effective assessing the activity of MutY holds significant biological and medical importance. Herein, the precise identification/excision capacity of MutY to mismatched G-A base pair of dsDNA chains and the DNA-template-dependant fluorescence behaviors of copper nano cluster (CuNCs) was exploited for the accurate sensing of active MutY. Hairpin DNA with G-A base mismatch was excised by MutY to produce dsDNA chains with repetitive AAT-TTA base pairs.
View Article and Find Full Text PDFWant 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!