Loading…
DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins
Mutation of the dye gene of Escherichia coli results in sensitivity of dyes, envelope protein changes, loss of expression of alkaline phosphatase, and reduced transcription of sex factor F genes. We have determined the DNA sequence of a 1.4-kilobase pair fragment encompassing the dye gene. The codin...
Saved in:
Published in: | The Journal of biological chemistry 1985-04, Vol.260 (7), p.4236-4242 |
---|---|
Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c463t-3e7bf0e8dce7b2ad6aa4f17867c93c913063b13857cd69a83d7142ddae18e49b3 |
---|---|
cites | cdi_FETCH-LOGICAL-c463t-3e7bf0e8dce7b2ad6aa4f17867c93c913063b13857cd69a83d7142ddae18e49b3 |
container_end_page | 4242 |
container_issue | 7 |
container_start_page | 4236 |
container_title | The Journal of biological chemistry |
container_volume | 260 |
creator | Drury, L S Buxton, R S |
description | Mutation of the dye gene of Escherichia coli results in sensitivity of dyes, envelope protein changes, loss of expression of alkaline phosphatase, and reduced transcription of sex factor F genes. We have determined the DNA sequence of a 1.4-kilobase pair fragment encompassing the dye gene. The coding sequence of dye was identified as an open reading frame coding for a protein of Mr 27,346. A sequence of 54 residues at the amino terminus was extremely acidic, with 12 aspartic plus glutamic acid residues and only 2 lysine plus arginine residues. A sequence of 19 adjacent residues near the center of the protein was identical, except for one mismatch, with a sequence in the OmpR protein, involved in controlling the amounts of the major outer membrane proteins OmpF and OmpC at the level of transcription. 28% of the Dye protein was homologous with OmpR. The positions of dye and ompR on the genetic map were indicative of a gene duplication. It seems likely, therefore, that the Dye and OmpR proteins are related, and Dye may thus be involved in the osmoregulation of envelope protein genes as well as being required for sex factor gene expression. The Dye protein itself, like OmpR, was shown not to be an envelope protein. A second open reading frame on the other DNA strand may use the same transcription termination site as dye. |
doi_str_mv | 10.1016/S0021-9258(18)89255-9 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76048352</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925818892559</els_id><sourcerecordid>76048352</sourcerecordid><originalsourceid>FETCH-LOGICAL-c463t-3e7bf0e8dce7b2ad6aa4f17867c93c913063b13857cd69a83d7142ddae18e49b3</originalsourceid><addsrcrecordid>eNqFkd9vFCEQgInR1LP1T2hCjGn0YRUWloUn0_SHmjQ2qZr4RliYvcXswgl7vdx_X653uVd5Ych8MwMfCJ1T8okSKj7_JKSmlaob-YHKj7IETaVeoAUlklWsoX9eosUReY3e5PyXlMUVPUEntZKcKrlAm-sflzjDvzUEC9gEM26zzzj2eB4Auy3gJQTYnW-yHSB5O3iDbRw9TvAIZszYTD5EbKx3eIhTHONyizuYNwDh2MQEh--n1QNepTiDD_kMvepLMbw97Kfo9-3Nr6tv1d391-9Xl3eV5YLNFYO26wlIZ0tQGyeM4T1tpWitYlZRRgTrKJNNa51QRjLXUl47Z4BK4Kpjp-hi37cMLo_Ms558tjCOJkBcZ90KwiVr6gI2e9CmmHOCXq-Sn0zaakr0Trh-Fq53NjWV-lm4VqXu_DBg3U3gjlUHwyX__pA32ZqxTyZYn4-Y5Iy1lBbs3R4b_HLY-AS687EIn3QtiG41r5ko0Jc9BMXYo4eks_W7j3OlwM7aRf-f2z4BrSao-w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76048352</pqid></control><display><type>article</type><title>DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins</title><source>BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS</source><creator>Drury, L S ; Buxton, R S</creator><creatorcontrib>Drury, L S ; Buxton, R S</creatorcontrib><description>Mutation of the dye gene of Escherichia coli results in sensitivity of dyes, envelope protein changes, loss of expression of alkaline phosphatase, and reduced transcription of sex factor F genes. We have determined the DNA sequence of a 1.4-kilobase pair fragment encompassing the dye gene. The coding sequence of dye was identified as an open reading frame coding for a protein of Mr 27,346. A sequence of 54 residues at the amino terminus was extremely acidic, with 12 aspartic plus glutamic acid residues and only 2 lysine plus arginine residues. A sequence of 19 adjacent residues near the center of the protein was identical, except for one mismatch, with a sequence in the OmpR protein, involved in controlling the amounts of the major outer membrane proteins OmpF and OmpC at the level of transcription. 28% of the Dye protein was homologous with OmpR. The positions of dye and ompR on the genetic map were indicative of a gene duplication. It seems likely, therefore, that the Dye and OmpR proteins are related, and Dye may thus be involved in the osmoregulation of envelope protein genes as well as being required for sex factor gene expression. The Dye protein itself, like OmpR, was shown not to be an envelope protein. A second open reading frame on the other DNA strand may use the same transcription termination site as dye.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)89255-9</identifier><identifier>PMID: 2984198</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - analysis ; Base Sequence ; Biological and medical sciences ; Biotechnology ; DNA, Bacterial - analysis ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Genes. Genome ; Genetic engineering ; Genetic technics ; Methods. Procedures. Technologies ; Molecular and cellular biology ; Molecular genetics ; Nucleic Acid Conformation ; Synthetic digonucleotides and genes. Sequencing</subject><ispartof>The Journal of biological chemistry, 1985-04, Vol.260 (7), p.4236-4242</ispartof><rights>1985 © 1985 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-3e7bf0e8dce7b2ad6aa4f17867c93c913063b13857cd69a83d7142ddae18e49b3</citedby><cites>FETCH-LOGICAL-c463t-3e7bf0e8dce7b2ad6aa4f17867c93c913063b13857cd69a83d7142ddae18e49b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8433711$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2984198$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Drury, L S</creatorcontrib><creatorcontrib>Buxton, R S</creatorcontrib><title>DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Mutation of the dye gene of Escherichia coli results in sensitivity of dyes, envelope protein changes, loss of expression of alkaline phosphatase, and reduced transcription of sex factor F genes. We have determined the DNA sequence of a 1.4-kilobase pair fragment encompassing the dye gene. The coding sequence of dye was identified as an open reading frame coding for a protein of Mr 27,346. A sequence of 54 residues at the amino terminus was extremely acidic, with 12 aspartic plus glutamic acid residues and only 2 lysine plus arginine residues. A sequence of 19 adjacent residues near the center of the protein was identical, except for one mismatch, with a sequence in the OmpR protein, involved in controlling the amounts of the major outer membrane proteins OmpF and OmpC at the level of transcription. 28% of the Dye protein was homologous with OmpR. The positions of dye and ompR on the genetic map were indicative of a gene duplication. It seems likely, therefore, that the Dye and OmpR proteins are related, and Dye may thus be involved in the osmoregulation of envelope protein genes as well as being required for sex factor gene expression. The Dye protein itself, like OmpR, was shown not to be an envelope protein. A second open reading frame on the other DNA strand may use the same transcription termination site as dye.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - analysis</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>DNA, Bacterial - analysis</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes. Genome</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Nucleic Acid Conformation</subject><subject>Synthetic digonucleotides and genes. Sequencing</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><recordid>eNqFkd9vFCEQgInR1LP1T2hCjGn0YRUWloUn0_SHmjQ2qZr4RliYvcXswgl7vdx_X653uVd5Ych8MwMfCJ1T8okSKj7_JKSmlaob-YHKj7IETaVeoAUlklWsoX9eosUReY3e5PyXlMUVPUEntZKcKrlAm-sflzjDvzUEC9gEM26zzzj2eB4Auy3gJQTYnW-yHSB5O3iDbRw9TvAIZszYTD5EbKx3eIhTHONyizuYNwDh2MQEh--n1QNepTiDD_kMvepLMbw97Kfo9-3Nr6tv1d391-9Xl3eV5YLNFYO26wlIZ0tQGyeM4T1tpWitYlZRRgTrKJNNa51QRjLXUl47Z4BK4Kpjp-hi37cMLo_Ms558tjCOJkBcZ90KwiVr6gI2e9CmmHOCXq-Sn0zaakr0Trh-Fq53NjWV-lm4VqXu_DBg3U3gjlUHwyX__pA32ZqxTyZYn4-Y5Iy1lBbs3R4b_HLY-AS687EIn3QtiG41r5ko0Jc9BMXYo4eks_W7j3OlwM7aRf-f2z4BrSao-w</recordid><startdate>19850410</startdate><enddate>19850410</enddate><creator>Drury, L S</creator><creator>Buxton, R S</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><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>7X8</scope></search><sort><creationdate>19850410</creationdate><title>DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins</title><author>Drury, L S ; Buxton, R S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-3e7bf0e8dce7b2ad6aa4f17867c93c913063b13857cd69a83d7142ddae18e49b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - analysis</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>DNA, Bacterial - analysis</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes. Genome</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Nucleic Acid Conformation</topic><topic>Synthetic digonucleotides and genes. Sequencing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Drury, L S</creatorcontrib><creatorcontrib>Buxton, R S</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Drury, L S</au><au>Buxton, R S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1985-04-10</date><risdate>1985</risdate><volume>260</volume><issue>7</issue><spage>4236</spage><epage>4242</epage><pages>4236-4242</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Mutation of the dye gene of Escherichia coli results in sensitivity of dyes, envelope protein changes, loss of expression of alkaline phosphatase, and reduced transcription of sex factor F genes. We have determined the DNA sequence of a 1.4-kilobase pair fragment encompassing the dye gene. The coding sequence of dye was identified as an open reading frame coding for a protein of Mr 27,346. A sequence of 54 residues at the amino terminus was extremely acidic, with 12 aspartic plus glutamic acid residues and only 2 lysine plus arginine residues. A sequence of 19 adjacent residues near the center of the protein was identical, except for one mismatch, with a sequence in the OmpR protein, involved in controlling the amounts of the major outer membrane proteins OmpF and OmpC at the level of transcription. 28% of the Dye protein was homologous with OmpR. The positions of dye and ompR on the genetic map were indicative of a gene duplication. It seems likely, therefore, that the Dye and OmpR proteins are related, and Dye may thus be involved in the osmoregulation of envelope protein genes as well as being required for sex factor gene expression. The Dye protein itself, like OmpR, was shown not to be an envelope protein. A second open reading frame on the other DNA strand may use the same transcription termination site as dye.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2984198</pmid><doi>10.1016/S0021-9258(18)89255-9</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9258 |
ispartof | The Journal of biological chemistry, 1985-04, Vol.260 (7), p.4236-4242 |
issn | 0021-9258 1083-351X |
language | eng |
recordid | cdi_proquest_miscellaneous_76048352 |
source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
subjects | Amino Acid Sequence Bacterial Proteins - analysis Base Sequence Biological and medical sciences Biotechnology DNA, Bacterial - analysis Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genes. Genome Genetic engineering Genetic technics Methods. Procedures. Technologies Molecular and cellular biology Molecular genetics Nucleic Acid Conformation Synthetic digonucleotides and genes. Sequencing |
title | DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-21T20%3A07%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=DNA%20sequence%20analysis%20of%20the%20dye%20gene%20of%20Escherichia%20coli%20reveals%20amino%20acid%20homology%20between%20the%20dye%20and%20OmpR%20proteins&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Drury,%20L%20S&rft.date=1985-04-10&rft.volume=260&rft.issue=7&rft.spage=4236&rft.epage=4242&rft.pages=4236-4242&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(18)89255-9&rft_dat=%3Cproquest_cross%3E76048352%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c463t-3e7bf0e8dce7b2ad6aa4f17867c93c913063b13857cd69a83d7142ddae18e49b3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=76048352&rft_id=info:pmid/2984198&rfr_iscdi=true |