<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Hahn J</submitter><funding>NIGMS NIH HHS</funding><pagination>202-15</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4429805</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>72(1)</volume><pubmed_abstract>During the development of transformability (competence), Bacillus subtilis synthesizes a set of proteins that mediate both the uptake of DNA at the cell poles and the recombination of this DNA with the resident chromosome. Most, if not all, of these Com proteins localize to the poles of the cell, where they associate with one another, and are then seen to delocalize as transformability declines. In this study, we use fluorescence microscopy to analyse the localization and delocalization processes. We show that localization most likely occurs by a diffusion-capture mechanism, not requiring metabolic energy, whereas delocalization is prevented in the presence of sodium azide. The kinetics of localization suggest that this process requires the synthesis of a critical protein or set of protein</pubmed_abstract><journal>Molecular microbiology</journal><pubmed_title>McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.</pubmed_title><pmcid>PMC4429805</pmcid><funding_grant_id>R01 GM057720</funding_grant_id><funding_grant_id>GM057720</funding_grant_id><funding_grant_id>R01 GM057720-38</funding_grant_id><pubmed_authors>Briley K</pubmed_authors><pubmed_authors>Kramer N</pubmed_authors><pubmed_authors>Dubnau D</pubmed_authors><pubmed_authors>Hahn J</pubmed_authors></additional><is_claimable>false</is_claimable><name>McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.</name><description>During the development of transformability (competence), Bacillus subtilis synthesizes a set of proteins that mediate both the uptake of DNA at the cell poles and the recombination of this DNA with the resident chromosome. Most, if not all, of these Com proteins localize to the poles of the cell, where they associate with one another, and are then seen to delocalize as transformability declines. In this study, we use fluorescence microscopy to analyse the localization and delocalization processes. We show that localization most likely occurs by a diffusion-capture mechanism, not requiring metabolic energy, whereas delocalization is prevented in the presence of sodium azide. The kinetics of localization suggest that this process requires the synthesis of a critical protein or set of protein</description><dates><release>2009-01-01T00:00:00Z</release><publication>2009 Apr</publication><modification>2025-04-04T00:28:36.978Z</modification><creation>2019-03-27T01:51:32Z</creation></dates><accession>S-EPMC4429805</accession><cross_references><pubmed>19226326</pubmed><doi>10.1111/j.1365-2958.2009.06636.x</doi></cross_references></HashMap>