One of the distinct characteristics of Gram-negative bacteria such as Escherichia coli is the possession of a double-membraned cell envelope. The outer membrane provides an additional layer of protection against hydrophobic molecules including antibiotics, contributing to the multidrug resistance crisis. The Gram-negative membrane is composed of phospholipids, glycolipids, and proteins. A large portion of the bacterial cellular proteome is composed of membrane proteins. Despite this, the functions of several membrane proteins are as yet undefined. Therefore, defining the physiological roles of uncharacterized membrane proteins is expected to provide us with insights into the biology of the Gram-negative cell envelope and to perhaps address aspects of bacterial multidrug resistance. In this thesis, I have characterized the genetic phenotypes of a predicted inner membrane lipoprotein of unknown function in E. coli, a model Gram-negative bacterium. The deletion of this putative lipoprotein confers pleiotropic phenotypes such as a reduction in cellular viability, morphology defects, and sensitivity to detergents and copper ions. The cell envelope stress response systems such as Rcs and Cpx cascades are upregulated in E. coli lacking the putative lipoprotein. Additionally, Cpx signaling is required for proliferation of the mutant under restrictive conditions. Further analyses suggest that the outer membrane protein biogenesis is compromised in this mutant, implying a physiological role for this predicted lipoprotein in outer membrane protein assembly. Taken together, these results suggest that this putative lipoprotein is involved in the maintenance of cell envelope integrity.
","abstract_html":"<p>One of the distinct characteristics of Gram-negative bacteria such as <em>Escherichia coli</em> is the possession of a double-membraned cell envelope. The outer membrane provides an additional layer of protection against hydrophobic molecules including antibiotics, contributing to the multidrug resistance crisis. The Gram-negative membrane is composed of phospholipids, glycolipids, and proteins. A large portion of the bacterial cellular proteome is composed of membrane proteins. Despite this, the functions of several membrane proteins are as yet undefined. Therefore, defining the physiological roles of uncharacterized membrane proteins is expected to provide us with insights into the biology of the Gram-negative cell envelope and to perhaps address aspects of bacterial multidrug resistance. In this thesis, I have characterized the genetic phenotypes of a predicted inner membrane lipoprotein of unknown function in <em>E. coli</em>, a model Gram-negative bacterium. The deletion of this putative lipoprotein confers pleiotropic phenotypes such as a reduction in cellular viability, morphology defects, and sensitivity to detergents and copper ions. The cell envelope stress response systems such as Rcs and Cpx cascades are upregulated in <em>E. coli</em> lacking the putative lipoprotein. Additionally, Cpx signaling is required for proliferation of the mutant under restrictive conditions. Further analyses suggest that the outer membrane protein biogenesis is compromised in this mutant, implying a physiological role for this predicted lipoprotein in outer membrane protein assembly. Taken together, these results suggest that this putative lipoprotein is involved in the maintenance of cell envelope integrity. </p>","abstract_has_math":false,"creators":["chung, charlie"],"institution":null,"degree_name":"Master of Science (M.S.)","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Anuradha Janakiraman","Christine Li","Shireen Saleque"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2018,"date_issued":"2018-01-01T08:00:00Z","date_published":"2018-01-01T08:00:00Z","updated_at":"2026-07-24T01:57:21Z","subjects":["cell envelope","membrane integrity","membrane biogenesis","protein biogenesis","lipoprotein","Biotechnology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://academicworks.cuny.edu/cc_etds_theses/737","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Anuradha Janakiraman","Christine Li","Shireen Saleque"]},{"key":"dc:creator","label":"Author","values":["chung, charlie"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2024-01-23T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science (M.S.)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["cell envelope","membrane integrity","membrane biogenesis","protein biogenesis","lipoprotein","Biotechnology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://academicworks.cuny.edu/cc_etds_theses/737"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["One of the distinct characteristics of Gram-negative bacteria such as Escherichia coli is the possession of a double-membraned cell envelope. The outer membrane provides an additional layer of protection against hydrophobic molecules including antibiotics, contributing to the multidrug resistance crisis. The Gram-negative membrane is composed of phospholipids, glycolipids, and proteins. A large portion of the bacterial cellular proteome is composed of membrane proteins. Despite this, the functions of several membrane proteins are as yet undefined. Therefore, defining the physiological roles of uncharacterized membrane proteins is expected to provide us with insights into the biology of the Gram-negative cell envelope and to perhaps address aspects of bacterial multidrug resistance. In this thesis, I have characterized the genetic phenotypes of a predicted inner membrane lipoprotein of unknown function in E. coli, a model Gram-negative bacterium. The deletion of this putative lipoprotein confers pleiotropic phenotypes such as a reduction in cellular viability, morphology defects, and sensitivity to detergents and copper ions. The cell envelope stress response systems such as Rcs and Cpx cascades are upregulated in E. coli lacking the putative lipoprotein. Additionally, Cpx signaling is required for proliferation of the mutant under restrictive conditions. Further analyses suggest that the outer membrane protein biogenesis is compromised in this mutant, implying a physiological role for this predicted lipoprotein in outer membrane protein assembly. Taken together, these results suggest that this putative lipoprotein is involved in the maintenance of cell envelope integrity.
"]},{"key":"dc:title","label":"Title","values":["A role for a predicted E. coli inner membrane lipoprotein in cell envelope integrity"]}]}],"canonical_facts":{"dc:contributor":["Anuradha Janakiraman","Christine Li","Shireen Saleque"],"dc:creator":["chung, charlie"],"dc:date.available":["2024-01-23T08:00:00Z"],"dc:description.abstract":["One of the distinct characteristics of Gram-negative bacteria such as Escherichia coli is the possession of a double-membraned cell envelope. The outer membrane provides an additional layer of protection against hydrophobic molecules including antibiotics, contributing to the multidrug resistance crisis. The Gram-negative membrane is composed of phospholipids, glycolipids, and proteins. A large portion of the bacterial cellular proteome is composed of membrane proteins. Despite this, the functions of several membrane proteins are as yet undefined. Therefore, defining the physiological roles of uncharacterized membrane proteins is expected to provide us with insights into the biology of the Gram-negative cell envelope and to perhaps address aspects of bacterial multidrug resistance. In this thesis, I have characterized the genetic phenotypes of a predicted inner membrane lipoprotein of unknown function in E. coli, a model Gram-negative bacterium. The deletion of this putative lipoprotein confers pleiotropic phenotypes such as a reduction in cellular viability, morphology defects, and sensitivity to detergents and copper ions. The cell envelope stress response systems such as Rcs and Cpx cascades are upregulated in E. coli lacking the putative lipoprotein. Additionally, Cpx signaling is required for proliferation of the mutant under restrictive conditions. Further analyses suggest that the outer membrane protein biogenesis is compromised in this mutant, implying a physiological role for this predicted lipoprotein in outer membrane protein assembly. Taken together, these results suggest that this putative lipoprotein is involved in the maintenance of cell envelope integrity.
"],"dc:identifier":["https://academicworks.cuny.edu/cc_etds_theses/737"],"dc:subject":["cell envelope","membrane integrity","membrane biogenesis","protein biogenesis","lipoprotein","Biotechnology"],"dc:title":["A role for a predicted E. coli inner membrane lipoprotein in cell envelope integrity"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science (M.S.)"]},"updated_at":"2026-07-24T01:57:21Z"}