ArticlePLoS biology2008
Group II intron protein localization and insertion sites are affected by polyphosphate.
Article in PLoS biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- An integrative multi-omics approach points to membrane composition as a key factor in E. coli persistence.PloS one · 2026Article
- Polyphosphate: The "Dark Matter" of Bacterial Chromatin Structure.Molecular microbiology · 2025Review
- Polyphosphate kinase deletion increases laboratory productivity in cyanobacteria.Frontiers in plant science · 2024Article
- Identification of Group II Intron RmInt1 Binding Sites in a Bacterial Genome.Frontiers in molecular biosciences · 2022Article
- Polyphosphate induces the proteolysis of ADP-bound fraction of initiator to inhibit DNA replication initiation upon stress in Escherichia coli.Nucleic acids research · 2020Article
- DNA and Polyphosphate in Directed Proteolysis for DNA Replication Control.Frontiers in microbiology · 2020Review
- Mobile Bacterial Group II Introns at the Crux of Eukaryotic Evolution.Microbiology spectrum · 2015Review
- Positively-charged semi-tunnel is a structural and surface characteristic of polyphosphate-binding proteins: an in-silico study.PloS one · 2015Article
- Horizontal transfer of bacterial polyphosphate kinases to eukaryotes: implications for the ice age and land colonisation.BMC research notes · 2013Article
- Genetic and biochemical assays reveal a key role for replication restart proteins in group II intron retrohoming.PLoS genetics · 2013Article
- Comparative transcriptional analysis of clinically relevant heat stress response in Clostridium difficile strain 630.PloS one · 2012Article
- Polyphosphate--an ancient energy source and active metabolic regulator.Microbial cell factories · 2011Review
- Group II introns: mobile ribozymes that invade DNA.Cold Spring Harbor perspectives in biology · 2011Review
- Phenotypic plasticity and effects of selection on cell division symmetry in Escherichia coli.PloS one · 2011Article
- High-throughput identification of protein localization dependency networks.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Human cell chips: adapting DNA microarray spotting technology to cell-based imaging assays.PloS one · 2009Article
- Global regulators orchestrate group II intron retromobility.Molecular cell · 2009Article
- EcI5, a group IIB intron with high retrohoming frequency: DNA target site recognition and use in gene targeting.RNA (New York, N.Y.) · 2009Article
- Systematic definition of protein constituents along the major polarization axis reveals an adaptive reuse of the polarization machinery in pheromone-treated budding yeast.Journal of proteome research · 2009Article
- The take and give between retrotransposable elements and their hosts.Annual review of genetics · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Mobile group II introns consist of a catalytic intron RNA and an intron-encoded protein with reverse transcriptase activity, which act together in a ribonucleoprotein particle to promote DNA integration during intron mobility. Previously, we found that the Lactococcus lactis Ll.LtrB intron-encoded protein (LtrA) expressed alone or with the intron RNA to form ribonucleoprotein particles localizes to bacterial cellular poles, potentially accounting for the intron's preferential insertion in the oriC and ter regions of the Escherichia coli chromosome. Here, by using cell microarrays and automated fluorescence microscopy to screen a transposon-insertion library, we identified five E. coli genes (gppA, uhpT, wcaK, ynbC, and zntR) whose disruption results in both an increased proportion of cells with more diffuse LtrA localization and a more uniform genomic distribution of Ll.LtrB-insertion sites. Surprisingly, we find that a common factor affecting LtrA localization in these and other disruptants is the accumulation of intracellular polyphosphate, which appears to bind LtrA and other basic proteins and delocalize them away from the poles. Our findings show that the intracellular localization of a group II intron-encoded protein is a major determinant of insertion-site preference. More generally, our results suggest that polyphosphate accumulation may provide a means of localizing proteins to different sites of action during cellular stress or entry into stationary phase, with potentially wide physiological consequences.
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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.