Gene duplication in bovine brain myelin proteolipid and homology with related proteins

Analysis of the amino acid sequence of bovine brain myelin proteolipid reveals not only extensive internal homology, but also homology with portions of the myelin basic protein, the peripheral nerve myelin protein, Po, and with the small proteolipid subunit of mitochondrial ATP synthase. These resul...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:FEBS letters 1983-09, Vol.161 (1), p.71-74
Hauptverfasser: Laursen, Richard A., Samiullah, Mohammed, Lees, Marjorie B.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 74
container_issue 1
container_start_page 71
container_title FEBS letters
container_volume 161
creator Laursen, Richard A.
Samiullah, Mohammed
Lees, Marjorie B.
description Analysis of the amino acid sequence of bovine brain myelin proteolipid reveals not only extensive internal homology, but also homology with portions of the myelin basic protein, the peripheral nerve myelin protein, Po, and with the small proteolipid subunit of mitochondrial ATP synthase. These results suggest that the myelin proteolipid gene has been constructed from a small number of genetic elements, and that these elements are also found in non-myelin proteins. Furthermore, the proteolipid appears to have evolved by acquisition of elements from a ‘gene pool’ over a period of time, rather than by a simple duplication mechanism.
doi_str_mv 10.1016/0014-5793(83)80732-7
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80611923</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0014579383807327</els_id><sourcerecordid>80611923</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4807-1e161617fc180313681a17688d68655ca65dccbc8bfa8818ab14fa6b6f2c168c3</originalsourceid><addsrcrecordid>eNqNkE1v1DAQhi0EKtvCPwApB4TgEPDEiTO5IEHVLUiVuABXy7En1MiJFzvbav89TrPaIyCPNJqZZz78MvYC-DvgIN9zDnXZtJ14g-It8lZUZfuIbQBbUYpa4mO2OSFP2XlKv3iOEbozdiYR60bwDftxTRMVdr_zzujZhalwU9GHO5ezfdQ5GA_ks9vFMFPwbudsoSdb3IYx-PDzUNy7-baI5PVMdqXclJ6xJ4P2iZ4f_QX7vr36dvm5vPl6_eXy401p6nxxCQQyv3YwgFyAkAga2nyclSibxmjZWGN6g_2gEQF1D_WgZS-HyoBEIy7Y63VuXvx7T2lWo0uGvNcThX1SyCVAV4l_gnl3V3eSZ7BeQRNDSpEGtYtu1PGggKtFd7WIqhZRFWZbdFdtbnt5nL_vR7KnpqPQuf7qWNfJaD9EPRmXTlgnGmgqmbHtit07T4f_Wq22V5-qpbDkUTxkl3s-rIMoq3_nKKpkHE2GrItkZmWD-_uH_gDonbG0</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>13694960</pqid></control><display><type>article</type><title>Gene duplication in bovine brain myelin proteolipid and homology with related proteins</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Laursen, Richard A. ; Samiullah, Mohammed ; Lees, Marjorie B.</creator><creatorcontrib>Laursen, Richard A. ; Samiullah, Mohammed ; Lees, Marjorie B.</creatorcontrib><description>Analysis of the amino acid sequence of bovine brain myelin proteolipid reveals not only extensive internal homology, but also homology with portions of the myelin basic protein, the peripheral nerve myelin protein, Po, and with the small proteolipid subunit of mitochondrial ATP synthase. These results suggest that the myelin proteolipid gene has been constructed from a small number of genetic elements, and that these elements are also found in non-myelin proteins. Furthermore, the proteolipid appears to have evolved by acquisition of elements from a ‘gene pool’ over a period of time, rather than by a simple duplication mechanism.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(83)80732-7</identifier><identifier>PMID: 6884530</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; ATP synthase ; Biological and medical sciences ; Brain - metabolism ; Cattle ; evolution ; Fundamental and applied biological sciences. Psychology ; Gene duplication ; Genes ; Genes. Genome ; membrane glycoproteins ; Membrane protein ; Molecular and cellular biology ; Molecular genetics ; myelin ; Myelin basic protein ; Myelin proteolipid ; Myelin Sheath - metabolism ; Nerve Tissue Proteins - genetics ; Po glycoprotein ; Proteolipids - genetics ; Structure-Activity Relationship</subject><ispartof>FEBS letters, 1983-09, Vol.161 (1), p.71-74</ispartof><rights>1983</rights><rights>FEBS Letters 161 (1983) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4807-1e161617fc180313681a17688d68655ca65dccbc8bfa8818ab14fa6b6f2c168c3</citedby><cites>FETCH-LOGICAL-c4807-1e161617fc180313681a17688d68655ca65dccbc8bfa8818ab14fa6b6f2c168c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579383807327$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=9351526$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6884530$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Laursen, Richard A.</creatorcontrib><creatorcontrib>Samiullah, Mohammed</creatorcontrib><creatorcontrib>Lees, Marjorie B.</creatorcontrib><title>Gene duplication in bovine brain myelin proteolipid and homology with related proteins</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Analysis of the amino acid sequence of bovine brain myelin proteolipid reveals not only extensive internal homology, but also homology with portions of the myelin basic protein, the peripheral nerve myelin protein, Po, and with the small proteolipid subunit of mitochondrial ATP synthase. These results suggest that the myelin proteolipid gene has been constructed from a small number of genetic elements, and that these elements are also found in non-myelin proteins. Furthermore, the proteolipid appears to have evolved by acquisition of elements from a ‘gene pool’ over a period of time, rather than by a simple duplication mechanism.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>ATP synthase</subject><subject>Biological and medical sciences</subject><subject>Brain - metabolism</subject><subject>Cattle</subject><subject>evolution</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene duplication</subject><subject>Genes</subject><subject>Genes. Genome</subject><subject>membrane glycoproteins</subject><subject>Membrane protein</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>myelin</subject><subject>Myelin basic protein</subject><subject>Myelin proteolipid</subject><subject>Myelin Sheath - metabolism</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Po glycoprotein</subject><subject>Proteolipids - genetics</subject><subject>Structure-Activity Relationship</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1v1DAQhi0EKtvCPwApB4TgEPDEiTO5IEHVLUiVuABXy7En1MiJFzvbav89TrPaIyCPNJqZZz78MvYC-DvgIN9zDnXZtJ14g-It8lZUZfuIbQBbUYpa4mO2OSFP2XlKv3iOEbozdiYR60bwDftxTRMVdr_zzujZhalwU9GHO5ezfdQ5GA_ks9vFMFPwbudsoSdb3IYx-PDzUNy7-baI5PVMdqXclJ6xJ4P2iZ4f_QX7vr36dvm5vPl6_eXy401p6nxxCQQyv3YwgFyAkAga2nyclSibxmjZWGN6g_2gEQF1D_WgZS-HyoBEIy7Y63VuXvx7T2lWo0uGvNcThX1SyCVAV4l_gnl3V3eSZ7BeQRNDSpEGtYtu1PGggKtFd7WIqhZRFWZbdFdtbnt5nL_vR7KnpqPQuf7qWNfJaD9EPRmXTlgnGmgqmbHtit07T4f_Wq22V5-qpbDkUTxkl3s-rIMoq3_nKKpkHE2GrItkZmWD-_uH_gDonbG0</recordid><startdate>19830905</startdate><enddate>19830905</enddate><creator>Laursen, Richard A.</creator><creator>Samiullah, Mohammed</creator><creator>Lees, Marjorie B.</creator><general>Elsevier B.V</general><general>Elsevier</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>7QL</scope><scope>7TK</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19830905</creationdate><title>Gene duplication in bovine brain myelin proteolipid and homology with related proteins</title><author>Laursen, Richard A. ; Samiullah, Mohammed ; Lees, Marjorie B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4807-1e161617fc180313681a17688d68655ca65dccbc8bfa8818ab14fa6b6f2c168c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>ATP synthase</topic><topic>Biological and medical sciences</topic><topic>Brain - metabolism</topic><topic>Cattle</topic><topic>evolution</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene duplication</topic><topic>Genes</topic><topic>Genes. Genome</topic><topic>membrane glycoproteins</topic><topic>Membrane protein</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>myelin</topic><topic>Myelin basic protein</topic><topic>Myelin proteolipid</topic><topic>Myelin Sheath - metabolism</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Po glycoprotein</topic><topic>Proteolipids - genetics</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Laursen, Richard A.</creatorcontrib><creatorcontrib>Samiullah, Mohammed</creatorcontrib><creatorcontrib>Lees, Marjorie B.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Laursen, Richard A.</au><au>Samiullah, Mohammed</au><au>Lees, Marjorie B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene duplication in bovine brain myelin proteolipid and homology with related proteins</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1983-09-05</date><risdate>1983</risdate><volume>161</volume><issue>1</issue><spage>71</spage><epage>74</epage><pages>71-74</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Analysis of the amino acid sequence of bovine brain myelin proteolipid reveals not only extensive internal homology, but also homology with portions of the myelin basic protein, the peripheral nerve myelin protein, Po, and with the small proteolipid subunit of mitochondrial ATP synthase. These results suggest that the myelin proteolipid gene has been constructed from a small number of genetic elements, and that these elements are also found in non-myelin proteins. Furthermore, the proteolipid appears to have evolved by acquisition of elements from a ‘gene pool’ over a period of time, rather than by a simple duplication mechanism.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>6884530</pmid><doi>10.1016/0014-5793(83)80732-7</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0014-5793
ispartof FEBS letters, 1983-09, Vol.161 (1), p.71-74
issn 0014-5793
1873-3468
language eng
recordid cdi_proquest_miscellaneous_80611923
source MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Amino Acid Sequence
Animals
ATP synthase
Biological and medical sciences
Brain - metabolism
Cattle
evolution
Fundamental and applied biological sciences. Psychology
Gene duplication
Genes
Genes. Genome
membrane glycoproteins
Membrane protein
Molecular and cellular biology
Molecular genetics
myelin
Myelin basic protein
Myelin proteolipid
Myelin Sheath - metabolism
Nerve Tissue Proteins - genetics
Po glycoprotein
Proteolipids - genetics
Structure-Activity Relationship
title Gene duplication in bovine brain myelin proteolipid and homology with related proteins
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T03%3A46%3A08IST&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=Gene%20duplication%20in%20bovine%20brain%20myelin%20proteolipid%20and%20homology%20with%20related%20proteins&rft.jtitle=FEBS%20letters&rft.au=Laursen,%20Richard%20A.&rft.date=1983-09-05&rft.volume=161&rft.issue=1&rft.spage=71&rft.epage=74&rft.pages=71-74&rft.issn=0014-5793&rft.eissn=1873-3468&rft.coden=FEBLAL&rft_id=info:doi/10.1016/0014-5793(83)80732-7&rft_dat=%3Cproquest_cross%3E80611923%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=13694960&rft_id=info:pmid/6884530&rft_els_id=0014579383807327&rfr_iscdi=true