Resistance and tolerance to foreign elements by prokaryotic immune systems - curating the genome.
Abstract
To engage in adaptive symbioses or genetic exchange, organisms must interact with foreign, non-self elements despite the risks of predation and parasitism. By surveying the interface between self and non-self, immune systems can help ensure the benevolence of these interactions without isolating their hosts altogether. In this Essay, we examine prokaryotic restriction-modification and CRISPR-Cas (clustered, regularly interspaced palindromic repeat-CRISPR-associated proteins) activities and discuss their analogy to mammalian immune pathways. We further explain how their capacities for resistance and tolerance are optimized to reduce parasitism and immunopathology during encounters with non-self.
References
A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes
Phages and the evolution of bacterial pathogens: from genomic rearrangements to lysogenic conversion
Citations
Related Concepts
Related Feeds
CRISPR for Genome Editing
Genome editing technologies enable the editing of genes to create or correct mutations. Clustered regularly interspaced short palindromic repeats (CRISPR) are DNA sequences in the genome that are recognized and cleaved by CRISPR-associated proteins (Cas). Here is the latest research on the use of CRISPR-Cas system in gene editing.
CRISPR Ribonucleases Deactivation
CRISPR-Cas system enables the editing of genes to create or correct mutations. This feed focuses on mechanisms that underlie deactivation of CRISPR ribonucleases. Here is the latest research.
CRISPR (general)
Clustered regularly interspaced short palindromic repeats (CRISPR) are DNA sequences in the genome that are recognized and cleaved by CRISPR-associated proteins (Cas). CRISPR-Cas system enables the editing of genes to create or correct mutations. Discover the latest research on CRISPR here.
Biophysics of CRISPR
This feed focuses on broad characteristics of the CRISPR system and the proteins associated with it.