ArticleJournal of bacteriology2015
Characterization and localization of the Campylobacter jejuni transformation system proteins CtsE, CtsP, and CtsX.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Genomic Analysis Points to Multiple Genetic Mechanisms for Non-TransformableMicroorganisms · 2024Article
- Cj0683 Is a Competence Protein Essential for Efficient Initialization of DNA Uptake inBiomolecules · 2023Article
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- "Take It or Leave It"-Factors Regulating Competence Development and DNA Uptake inInternational journal of molecular sciences · 2021Article
- Natural Transformation as a Mechanism of Horizontal Gene Transfer inPathogens (Basel, Switzerland) · 2021Article
- Natural Competence and Horizontal Gene Transfer in Campylobacter.Current topics in microbiology and immunology · 2021Article
- Campylobacter jejuni: collective components promoting a successful enteric lifestyle.Nature reviews. Microbiology · 2018Review
- Methylation-dependent DNA discrimination in natural transformation ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The human pathogen Campylobacter jejuni is naturally competent for transformation with its own DNA. Genes required for efficient transformation in C. jejuni include those similar to components of type II secretion systems found in many Gram-negative bacteria (R. S. Wiesner, D. R. Hendrixson, and V. J. DiRita, J Bacteriol 185:5408-5418, 2003, http://dx.doi.org/10.1128/JB.185.18.5408-5418.2003). Two of these, ctsE and ctsP, encode proteins annotated as putative nucleotide binding nucleoside triphosphatases (NTPases) or nucleoside triphosphate (NTP) binding proteins. Here we demonstrate that the nucleotide binding motifs of both proteins are essential for their function in transformation of C. jejuni. Localization experiments demonstrated that CtsE is a soluble protein while CtsP is membrane associated in C. jejuni. A bacterial two-hybrid screen identified an interaction between CtsP and CtsX, an integral membrane protein also required for transformation. Topological analysis of CtsX by the use of LacZ and PhoA fusions demonstrated it to be a bitopic, integral membrane protein with a cytoplasmic amino terminus and a periplasmic carboxyl terminus. Notwithstanding its interaction with membrane-localized CtsX, CtsP inherently associates with the membrane, requiring neither CtsX nor several other Cts proteins for this association.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.