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Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli
Although bacteria have diverse membrane proteins, the function of many of them remains unknown or uncertain even in Escherichia coli . In this study, to investigate the function of hypothetical membrane proteins, genome-wide analysis of phenotypes of hypothetical membrane proteins was performed unde...
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| Published in: | The journal of microbiology 2020, 58(7), , pp.598-605 |
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| cites | cdi_FETCH-LOGICAL-c406t-321962bb3a47beee26d237e94459cbfc48bc6abb072c2002340605057e3a7e023 |
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| container_title | The journal of microbiology |
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| creator | Sung, Chul Gi Choi, Umji Lee, Chang-Ro |
| description | Although bacteria have diverse membrane proteins, the function of many of them remains unknown or uncertain even in
Escherichia coli
. In this study, to investigate the function of hypothetical membrane proteins, genome-wide analysis of phenotypes of hypothetical membrane proteins was performed under various envelope stresses. Several genes responsible for adaptation to envelope stresses were identified. Among them, deletion of YhcB, a conserved inner membrane protein of unknown function, caused high sensitivities to various envelope stresses and increased membrane permeability, and caused growth defect under normal growth conditions. Furthermore,
yhcB
deletion resulted in morphological aberration, such as branched shape, and cell division defects, such as filamentous growth and the generation of chromosome-less cells. The analysis of antibiotic susceptibility showed that the
yhcB
mutant was highly susceptible to various anti-folate antibiotics. Notably, all phenotypes of the
yhcB
mutant were completely or significantly restored by YhcB without the transmembrane domain, indicating that the localization of YhcB on the inner membrane is dispensable for its function. Taken together, our results demonstrate that YhcB is involved in cell morphology and cell division in a membrane localization-independent manner. |
| doi_str_mv | 10.1007/s12275-020-0078-4 |
| format | article |
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Escherichia coli
. In this study, to investigate the function of hypothetical membrane proteins, genome-wide analysis of phenotypes of hypothetical membrane proteins was performed under various envelope stresses. Several genes responsible for adaptation to envelope stresses were identified. Among them, deletion of YhcB, a conserved inner membrane protein of unknown function, caused high sensitivities to various envelope stresses and increased membrane permeability, and caused growth defect under normal growth conditions. Furthermore,
yhcB
deletion resulted in morphological aberration, such as branched shape, and cell division defects, such as filamentous growth and the generation of chromosome-less cells. The analysis of antibiotic susceptibility showed that the
yhcB
mutant was highly susceptible to various anti-folate antibiotics. Notably, all phenotypes of the
yhcB
mutant were completely or significantly restored by YhcB without the transmembrane domain, indicating that the localization of YhcB on the inner membrane is dispensable for its function. Taken together, our results demonstrate that YhcB is involved in cell morphology and cell division in a membrane localization-independent manner.</description><identifier>ISSN: 1225-8873</identifier><identifier>EISSN: 1976-3794</identifier><identifier>DOI: 10.1007/s12275-020-0078-4</identifier><identifier>PMID: 32323199</identifier><language>eng</language><publisher>Seoul: The Microbiological Society of Korea</publisher><subject>Adaptation ; Anti-Bacterial Agents - pharmacology ; Antibiotics ; Biomedical and Life Sciences ; Cell division ; Cell Division - genetics ; Cell Membrane - genetics ; Cell Membrane Permeability - genetics ; Cell morphology ; Chromosomes ; Coliforms ; Cytology ; Defects ; Deletion ; E coli ; Escherichia coli ; Escherichia coli - drug effects ; Escherichia coli - genetics ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Folic acid ; Gene Deletion ; Genes ; Genomes ; Growth conditions ; Life Sciences ; Localization ; Membrane permeability ; Membrane proteins ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Microbial Physiology and Biochemistry ; Microbial Sensitivity Tests ; Microbiology ; Morphology ; Mutants ; Oxidoreductases - genetics ; Oxidoreductases - metabolism ; Permeability ; Phenotype ; Phenotypes ; Proteins ; Stress, Physiological - genetics ; Stresses ; 생물학</subject><ispartof>The Journal of Microbiology, 2020, 58(7), , pp.598-605</ispartof><rights>The Microbiological Society of Korea 2020</rights><rights>The Microbiological Society of Korea 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-321962bb3a47beee26d237e94459cbfc48bc6abb072c2002340605057e3a7e023</citedby><cites>FETCH-LOGICAL-c406t-321962bb3a47beee26d237e94459cbfc48bc6abb072c2002340605057e3a7e023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32323199$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002599860$$DAccess content in National Research Foundation of Korea (NRF)$$Hfree_for_read</backlink></links><search><creatorcontrib>Sung, Chul Gi</creatorcontrib><creatorcontrib>Choi, Umji</creatorcontrib><creatorcontrib>Lee, Chang-Ro</creatorcontrib><title>Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli</title><title>The journal of microbiology</title><addtitle>J Microbiol</addtitle><addtitle>J Microbiol</addtitle><description>Although bacteria have diverse membrane proteins, the function of many of them remains unknown or uncertain even in
Escherichia coli
. In this study, to investigate the function of hypothetical membrane proteins, genome-wide analysis of phenotypes of hypothetical membrane proteins was performed under various envelope stresses. Several genes responsible for adaptation to envelope stresses were identified. Among them, deletion of YhcB, a conserved inner membrane protein of unknown function, caused high sensitivities to various envelope stresses and increased membrane permeability, and caused growth defect under normal growth conditions. Furthermore,
yhcB
deletion resulted in morphological aberration, such as branched shape, and cell division defects, such as filamentous growth and the generation of chromosome-less cells. The analysis of antibiotic susceptibility showed that the
yhcB
mutant was highly susceptible to various anti-folate antibiotics. Notably, all phenotypes of the
yhcB
mutant were completely or significantly restored by YhcB without the transmembrane domain, indicating that the localization of YhcB on the inner membrane is dispensable for its function. Taken together, our results demonstrate that YhcB is involved in cell morphology and cell division in a membrane localization-independent manner.</description><subject>Adaptation</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibiotics</subject><subject>Biomedical and Life Sciences</subject><subject>Cell division</subject><subject>Cell Division - genetics</subject><subject>Cell Membrane - genetics</subject><subject>Cell Membrane Permeability - genetics</subject><subject>Cell morphology</subject><subject>Chromosomes</subject><subject>Coliforms</subject><subject>Cytology</subject><subject>Defects</subject><subject>Deletion</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Folic acid</subject><subject>Gene Deletion</subject><subject>Genes</subject><subject>Genomes</subject><subject>Growth conditions</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Membrane permeability</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Microbial Physiology and Biochemistry</subject><subject>Microbial Sensitivity Tests</subject><subject>Microbiology</subject><subject>Morphology</subject><subject>Mutants</subject><subject>Oxidoreductases - genetics</subject><subject>Oxidoreductases - metabolism</subject><subject>Permeability</subject><subject>Phenotype</subject><subject>Phenotypes</subject><subject>Proteins</subject><subject>Stress, Physiological - genetics</subject><subject>Stresses</subject><subject>생물학</subject><issn>1225-8873</issn><issn>1976-3794</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp1kElLBDEQhYMo7j_AiwQ8eWjN1p3uow4uA4Ii40EvIclU21EnGZMeQX-9GdvlJDlUivreq-IhtEfJESVEHifKmCwLwkiR27oQK2iTNrIquGzEav4zVhZ1LfkG2krpiZCKcsHW0QZn-dGm2UQPNx340L_PncW201HbHqL70L0LHocWa2yDTxDfYIqd9xDxDGYmag94HkMPzuP7zp7mGT5Ltsta27ml6MXtoLVWvyTY_a7b6O78bDK6LK6uL8ajk6vCClL1BWe0qZgxXAtpAIBVU8YlNEKUjTWtFbWxlTaGSGYZIYxnFSlJKYFrCbnfRoeDr4-terZOBe2-6mNQz1Gd3E7GqilzSFRk9mBg8_GvC0i9egqL6PN5igkq67qiRGaKDpSNIaUIrZpHN9PxXVGilsmrIXmVTdUyebV03v92XpgZTH8VP1FngA1AyiP_CPFv9f-un1XGjPs</recordid><startdate>20200701</startdate><enddate>20200701</enddate><creator>Sung, Chul Gi</creator><creator>Choi, Umji</creator><creator>Lee, Chang-Ro</creator><general>The Microbiological Society of Korea</general><general>Springer Nature B.V</general><general>한국미생물학회</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7TN</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H94</scope><scope>H95</scope><scope>K9.</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>ACYCR</scope></search><sort><creationdate>20200701</creationdate><title>Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli</title><author>Sung, Chul Gi ; Choi, Umji ; Lee, Chang-Ro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-321962bb3a47beee26d237e94459cbfc48bc6abb072c2002340605057e3a7e023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Adaptation</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibiotics</topic><topic>Biomedical and Life Sciences</topic><topic>Cell division</topic><topic>Cell Division - genetics</topic><topic>Cell Membrane - genetics</topic><topic>Cell Membrane Permeability - genetics</topic><topic>Cell morphology</topic><topic>Chromosomes</topic><topic>Coliforms</topic><topic>Cytology</topic><topic>Defects</topic><topic>Deletion</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Folic acid</topic><topic>Gene Deletion</topic><topic>Genes</topic><topic>Genomes</topic><topic>Growth conditions</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Membrane permeability</topic><topic>Membrane proteins</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membranes</topic><topic>Microbial Physiology and Biochemistry</topic><topic>Microbial Sensitivity Tests</topic><topic>Microbiology</topic><topic>Morphology</topic><topic>Mutants</topic><topic>Oxidoreductases - genetics</topic><topic>Oxidoreductases - metabolism</topic><topic>Permeability</topic><topic>Phenotype</topic><topic>Phenotypes</topic><topic>Proteins</topic><topic>Stress, Physiological - genetics</topic><topic>Stresses</topic><topic>생물학</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sung, Chul Gi</creatorcontrib><creatorcontrib>Choi, Umji</creatorcontrib><creatorcontrib>Lee, Chang-Ro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oceanic Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Korean Citation Index</collection><jtitle>The journal of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sung, Chul Gi</au><au>Choi, Umji</au><au>Lee, Chang-Ro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli</atitle><jtitle>The journal of microbiology</jtitle><stitle>J Microbiol</stitle><addtitle>J Microbiol</addtitle><date>2020-07-01</date><risdate>2020</risdate><volume>58</volume><issue>7</issue><spage>598</spage><epage>605</epage><pages>598-605</pages><issn>1225-8873</issn><eissn>1976-3794</eissn><abstract>Although bacteria have diverse membrane proteins, the function of many of them remains unknown or uncertain even in
Escherichia coli
. In this study, to investigate the function of hypothetical membrane proteins, genome-wide analysis of phenotypes of hypothetical membrane proteins was performed under various envelope stresses. Several genes responsible for adaptation to envelope stresses were identified. Among them, deletion of YhcB, a conserved inner membrane protein of unknown function, caused high sensitivities to various envelope stresses and increased membrane permeability, and caused growth defect under normal growth conditions. Furthermore,
yhcB
deletion resulted in morphological aberration, such as branched shape, and cell division defects, such as filamentous growth and the generation of chromosome-less cells. The analysis of antibiotic susceptibility showed that the
yhcB
mutant was highly susceptible to various anti-folate antibiotics. Notably, all phenotypes of the
yhcB
mutant were completely or significantly restored by YhcB without the transmembrane domain, indicating that the localization of YhcB on the inner membrane is dispensable for its function. Taken together, our results demonstrate that YhcB is involved in cell morphology and cell division in a membrane localization-independent manner.</abstract><cop>Seoul</cop><pub>The Microbiological Society of Korea</pub><pmid>32323199</pmid><doi>10.1007/s12275-020-0078-4</doi><tpages>8</tpages></addata></record> |
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| ispartof | The Journal of Microbiology, 2020, 58(7), , pp.598-605 |
| issn | 1225-8873 1976-3794 |
| language | eng |
| recordid | cdi_nrf_kci_oai_kci_go_kr_ARTI_9502014 |
| source | Springer Nature |
| subjects | Adaptation Anti-Bacterial Agents - pharmacology Antibiotics Biomedical and Life Sciences Cell division Cell Division - genetics Cell Membrane - genetics Cell Membrane Permeability - genetics Cell morphology Chromosomes Coliforms Cytology Defects Deletion E coli Escherichia coli Escherichia coli - drug effects Escherichia coli - genetics Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Folic acid Gene Deletion Genes Genomes Growth conditions Life Sciences Localization Membrane permeability Membrane proteins Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Microbial Physiology and Biochemistry Microbial Sensitivity Tests Microbiology Morphology Mutants Oxidoreductases - genetics Oxidoreductases - metabolism Permeability Phenotype Phenotypes Proteins Stress, Physiological - genetics Stresses 생물학 |
| title | Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli |
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