<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Falchi FA</submitter><funding>Università degli Studi di Napoli Federico II</funding><funding>Università degli Studì di Milano</funding><pagination>E826</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7356881</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(6)</volume><pubmed_abstract>LpxT is an inner membrane protein that transfers a phosphate group from the essential lipid undecaprenyl pyrophosphate (C-55PP) to the lipid A moiety of lipopolysaccharide, generating a lipid A &lt;i>tris&lt;/i>-phosphorylated species. The protein is encoded by the non-essential &lt;i>lpxT&lt;/i> gene, which is conserved in distantly related Gram-negative bacteria. In this work, we investigated the phenotypic effect of &lt;i>lpxT&lt;/i> ectopic expression from a plasmid in &lt;i>Escherichia coli&lt;/i>. We found that &lt;i>lpxT&lt;/i> induction inhibited cell division and led to the formation of elongated cells, mostly with absent or altered septa. Moreover, the cells became sensitive to detergents and to hypo-osmotic shock, indicating that they had cell envelope defects. These effects were not due to lipid A hyperphos</pubmed_abstract><journal>Microorganisms</journal><pubmed_title>Overexpression of &lt;i>lpxT&lt;/i> Gene in &lt;i>Escherichia coli&lt;/i> Inhibits Cell Division and Causes Envelope Defects without Changing the Overall Phosphorylation Level of Lipid A.</pubmed_title><pmcid>PMC7356881</pmcid><funding_grant_id>E66C18001330003</funding_grant_id><funding_grant_id>na</funding_grant_id><pubmed_authors>Molinaro A</pubmed_authors><pubmed_authors>Briani F</pubmed_authors><pubmed_authors>Paroni M</pubmed_authors><pubmed_authors>Falchi FA</pubmed_authors><pubmed_authors>Di Lorenzo F</pubmed_authors><pubmed_authors>Pizzoccheri R</pubmed_authors><pubmed_authors>Forti F</pubmed_authors><pubmed_authors>Casino G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Overexpression of &lt;i>lpxT&lt;/i> Gene in &lt;i>Escherichia coli&lt;/i> Inhibits Cell Division and Causes Envelope Defects without Changing the Overall Phosphorylation Level of Lipid A.</name><description>LpxT is an inner membrane protein that transfers a phosphate group from the essential lipid undecaprenyl pyrophosphate (C-55PP) to the lipid A moiety of lipopolysaccharide, generating a lipid A &lt;i>tris&lt;/i>-phosphorylated species. The protein is encoded by the non-essential &lt;i>lpxT&lt;/i> gene, which is conserved in distantly related Gram-negative bacteria. In this work, we investigated the phenotypic effect of &lt;i>lpxT&lt;/i> ectopic expression from a plasmid in &lt;i>Escherichia coli&lt;/i>. We found that &lt;i>lpxT&lt;/i> induction inhibited cell division and led to the formation of elongated cells, mostly with absent or altered septa. Moreover, the cells became sensitive to detergents and to hypo-osmotic shock, indicating that they had cell envelope defects. These effects were not due to lipid A hyperphos</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 May</publication><modification>2026-04-29T08:43:46.4Z</modification><creation>2026-04-14T03:06:45.763Z</creation></dates><accession>S-EPMC7356881</accession><cross_references><pubmed>32486329</pubmed><doi>10.3390/microorganisms8060826</doi></cross_references></HashMap>