<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Hayes S</submitter><funding>Natural Sciences and Engineering Research Council of Canada</funding><pagination>E172</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4926192</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(6)</volume><pubmed_abstract>The bacteriophage lambda replication initiation protein P exhibits a toxic effect on its Escherichia coli (E. coli) host, likely due to the formation of a dead-end P-DnaB complex, sequestering the replicative DnaB helicase from further activity. Intracellular expression of P triggers SOS-independent cellular filamentation and rapidly cures resident ColE1 plasmids. The toxicity of P is suppressed by alleles of P or dnaB. We asked whether P buildup within a cell can influence E. coli replication fidelity. The influence of P expression from a defective prophage, or when cloned and expressed from a plasmid was examined by screening for auxotrophic mutants, or by selection for rifampicin resistant (Rif(R)) cells acquiring mutations within the rpoB gene encoding the β-subunit of RNA polymerase (</pubmed_abstract><journal>Viruses</journal><pubmed_title>Lambda gpP-DnaB Helicase Sequestration and gpP-RpoB Associated Effects: On Screens for Auxotrophs, Selection for Rif(R), Toxicity, Mutagenicity, Plasmid Curing.</pubmed_title><pmcid>PMC4926192</pmcid><funding_grant_id>138296-2012</funding_grant_id><pubmed_authors>Chu A</pubmed_authors><pubmed_authors>Wang W</pubmed_authors><pubmed_authors>Hayes S</pubmed_authors><pubmed_authors>Rajamanickam K</pubmed_authors><pubmed_authors>Banerjee A</pubmed_authors><pubmed_authors>Hayes C</pubmed_authors></additional><is_claimable>false</is_claimable><name>Lambda gpP-DnaB Helicase Sequestration and gpP-RpoB Associated Effects: On Screens for Auxotrophs, Selection for Rif(R), Toxicity, Mutagenicity, Plasmid Curing.</name><description>The bacteriophage lambda replication initiation protein P exhibits a toxic effect on its Escherichia coli (E. coli) host, likely due to the formation of a dead-end P-DnaB complex, sequestering the replicative DnaB helicase from further activity. Intracellular expression of P triggers SOS-independent cellular filamentation and rapidly cures resident ColE1 plasmids. The toxicity of P is suppressed by alleles of P or dnaB. We asked whether P buildup within a cell can influence E. coli replication fidelity. The influence of P expression from a defective prophage, or when cloned and expressed from a plasmid was examined by screening for auxotrophic mutants, or by selection for rifampicin resistant (Rif(R)) cells acquiring mutations within the rpoB gene encoding the β-subunit of RNA polymerase (</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Jun</publication><modification>2026-07-16T02:28:07.551Z</modification><creation>2019-03-27T02:17:09Z</creation></dates><accession>S-EPMC4926192</accession><cross_references><pubmed>27338450</pubmed><doi>10.3390/v8060172</doi></cross_references></HashMap>