Amino-acid sequence of scylliorhinine Z1 and comparison of the primary structure of the protamines of the dogfish Scylliorhinus caniculus
Identifieur interne : 000754 ( Istex/Corpus ); précédent : 000753; suivant : 000755Amino-acid sequence of scylliorhinine Z1 and comparison of the primary structure of the protamines of the dogfish Scylliorhinus caniculus
Auteurs : Philippe Chevaillier ; Arlette Martinage ; Michel Gusse ; Pierre SautièreSource :
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology [ 0167-4838 ] ; 1987.
Abstract
Scylliorhinine Z1 is one of the four protamines of mature sperm nuclei of the dogfish. This protein has a high content of arginine and cysteine and the polypeptide chain contains 50 residues. These molecular characteristics are also found in mammalian protamines, but differ from those of teleost protamines. The amino-acid sequence reveals that the N-terminal half is enriched in hydrophobic amino acids, whereas the C-terminal domain is more basic and contains a cluster of four hydroxylated amino acids. A sequence of eight amino acids is duplicated. The protein remains monophosphorylated in mature sperm nuclei. The amino-acid sequence reveals no clear homology with teleost protamines. Moreover, the four scylliorhinines could play specific functions in DNA packaging, as they do not appear to be structurally related. Therefore, they cannot be considered as being derived from a unique ancestral gene, as has been suggested for teleost protamines.
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DOI: 10.1016/0167-4838(87)90156-7
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CNRS No. 409, Institut de Recherches sur le Cancer, Place de Verdun, Lille France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title><title level="j" type="abbrev">BBAPRO</title><idno type="ISSN">0167-4838</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">914</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="19">19</biblScope><biblScope unit="page" to="27">27</biblScope></imprint><idno type="ISSN">0167-4838</idno></series><idno type="istex">D13E979A05FA69D0E2DC1CEEAC7EB9421092D418</idno><idno type="DOI">10.1016/0167-4838(87)90156-7</idno><idno type="PII">0167-4838(87)90156-7</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-4838</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Scylliorhinine Z1 is one of the four protamines of mature sperm nuclei of the dogfish. This protein has a high content of arginine and cysteine and the polypeptide chain contains 50 residues. These molecular characteristics are also found in mammalian protamines, but differ from those of teleost protamines. The amino-acid sequence reveals that the N-terminal half is enriched in hydrophobic amino acids, whereas the C-terminal domain is more basic and contains a cluster of four hydroxylated amino acids. A sequence of eight amino acids is duplicated. The protein remains monophosphorylated in mature sperm nuclei. The amino-acid sequence reveals no clear homology with teleost protamines. Moreover, the four scylliorhinines could play specific functions in DNA packaging, as they do not appear to be structurally related. Therefore, they cannot be considered as being derived from a unique ancestral gene, as has been suggested for teleost protamines.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Philippe Chevaillier</name><affiliations><json:string>Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, Créteil France</json:string><json:string>Correspondence: Ph. Chevaillier, Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, 94010 Créteil, France.</json:string></affiliations></json:item><json:item><name>Arlette Martinage</name><affiliations><json:string>U.A. CNRS No. 409, Institut de Recherches sur le Cancer, Place de Verdun, Lille France</json:string></affiliations></json:item><json:item><name>Michel Gusse</name><affiliations><json:string>Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, Créteil France</json:string></affiliations></json:item><json:item><name>Pierre Sautière</name><affiliations><json:string>U.A. 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Chevaillier, Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, 94010 Créteil, France.</affiliation></author><author xml:id="author-2"><persName><forename type="first">Arlette</forename><surname>Martinage</surname></persName><affiliation>U.A. CNRS No. 409, Institut de Recherches sur le Cancer, Place de Verdun, Lille France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Michel</forename><surname>Gusse</surname></persName><affiliation>Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, Créteil France</affiliation></author><author xml:id="author-4"><persName><forename type="first">Pierre</forename><surname>Sautière</surname></persName><affiliation>U.A. CNRS No. 409, Institut de Recherches sur le Cancer, Place de Verdun, Lille France</affiliation></author></analytic><monogr><title level="j">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title><title level="j" type="abbrev">BBAPRO</title><idno type="pISSN">0167-4838</idno><idno type="PII">S0167-4838(00)X0148-3</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987"></date><biblScope unit="volume">914</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="19">19</biblScope><biblScope unit="page" to="27">27</biblScope></imprint></monogr><idno type="istex">D13E979A05FA69D0E2DC1CEEAC7EB9421092D418</idno><idno type="DOI">10.1016/0167-4838(87)90156-7</idno><idno type="PII">0167-4838(87)90156-7</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1987</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Scylliorhinine Z1 is one of the four protamines of mature sperm nuclei of the dogfish. This protein has a high content of arginine and cysteine and the polypeptide chain contains 50 residues. These molecular characteristics are also found in mammalian protamines, but differ from those of teleost protamines. The amino-acid sequence reveals that the N-terminal half is enriched in hydrophobic amino acids, whereas the C-terminal domain is more basic and contains a cluster of four hydroxylated amino acids. A sequence of eight amino acids is duplicated. The protein remains monophosphorylated in mature sperm nuclei. The amino-acid sequence reveals no clear homology with teleost protamines. Moreover, the four scylliorhinines could play specific functions in DNA packaging, as they do not appear to be structurally related. Therefore, they cannot be considered as being derived from a unique ancestral gene, as has been suggested for teleost protamines.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Scylliorhinine Z1</term></item><item><term>Protamine</term></item><item><term>Nuclear basic protein</term></item><item><term>Sperm chromatin</term></item><item><term>Amino acid sequence</term></item><item><term>(Dogfish)</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1987">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/D13E979A05FA69D0E2DC1CEEAC7EB9421092D418/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>BBAPRO</jid><aid>87901567</aid><ce:pii>0167-4838(87)90156-7</ce:pii><ce:doi>10.1016/0167-4838(87)90156-7</ce:doi><ce:copyright type="unknown" year="1987"></ce:copyright></item-info><head><ce:title>Amino-acid sequence of scylliorhinine Z1 and comparison of the primary structure of the protamines of the dogfish <ce:italic>Scylliorhinus caniculus</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>Philippe</ce:given-name><ce:surname>Chevaillier</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Arlette</ce:given-name><ce:surname>Martinage</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Michel</ce:given-name><ce:surname>Gusse</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Pierre</ce:given-name><ce:surname>Sautière</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, Créteil France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>U.A. CNRS No. 409, Institut de Recherches sur le Cancer, Place de Verdun, Lille France</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Correspondence: Ph. Chevaillier, Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, 94010 Créteil, France.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="9" month="3" year="1987"></ce:date-received><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Scylliorhinine Z1 is one of the four protamines of mature sperm nuclei of the dogfish. This protein has a high content of arginine and cysteine and the polypeptide chain contains 50 residues. These molecular characteristics are also found in mammalian protamines, but differ from those of teleost protamines. The amino-acid sequence reveals that the N-terminal half is enriched in hydrophobic amino acids, whereas the C-terminal domain is more basic and contains a cluster of four hydroxylated amino acids. A sequence of eight amino acids is duplicated. The protein remains monophosphorylated in mature sperm nuclei. The amino-acid sequence reveals no clear homology with teleost protamines. Moreover, the four scylliorhinines could play specific functions in DNA packaging, as they do not appear to be structurally related. Therefore, they cannot be considered as being derived from a unique ancestral gene, as has been suggested for teleost protamines.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Scylliorhinine Z1</ce:text></ce:keyword><ce:keyword><ce:text>Protamine</ce:text></ce:keyword><ce:keyword><ce:text>Nuclear basic protein</ce:text></ce:keyword><ce:keyword><ce:text>Sperm chromatin</ce:text></ce:keyword><ce:keyword><ce:text>Amino acid sequence</ce:text></ce:keyword><ce:keyword><ce:text>(Dogfish)</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Amino-acid sequence of scylliorhinine Z1 and comparison of the primary structure of the protamines of the dogfish Scylliorhinus caniculus</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Amino-acid sequence of scylliorhinine Z1 and comparison of the primary structure of the protamines of the dogfish</title></titleInfo><name type="personal"><namePart type="given">Philippe</namePart><namePart type="family">Chevaillier</namePart><affiliation>Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, Créteil France</affiliation><affiliation>Correspondence: Ph. Chevaillier, Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, 94010 Créteil, France.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Arlette</namePart><namePart type="family">Martinage</namePart><affiliation>U.A. CNRS No. 409, Institut de Recherches sur le Cancer, Place de Verdun, Lille France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michel</namePart><namePart type="family">Gusse</namePart><affiliation>Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, Créteil France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Pierre</namePart><namePart type="family">Sautière</namePart><affiliation>U.A. CNRS No. 409, Institut de Recherches sur le Cancer, Place de Verdun, Lille France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1987</dateIssued><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Scylliorhinine Z1 is one of the four protamines of mature sperm nuclei of the dogfish. This protein has a high content of arginine and cysteine and the polypeptide chain contains 50 residues. These molecular characteristics are also found in mammalian protamines, but differ from those of teleost protamines. The amino-acid sequence reveals that the N-terminal half is enriched in hydrophobic amino acids, whereas the C-terminal domain is more basic and contains a cluster of four hydroxylated amino acids. A sequence of eight amino acids is duplicated. The protein remains monophosphorylated in mature sperm nuclei. The amino-acid sequence reveals no clear homology with teleost protamines. Moreover, the four scylliorhinines could play specific functions in DNA packaging, as they do not appear to be structurally related. Therefore, they cannot be considered as being derived from a unique ancestral gene, as has been suggested for teleost protamines.</abstract><subject><genre>Keywords</genre><topic>Scylliorhinine Z1</topic><topic>Protamine</topic><topic>Nuclear basic protein</topic><topic>Sperm chromatin</topic><topic>Amino acid sequence</topic><topic>(Dogfish)</topic></subject><relatedItem type="host"><titleInfo><title>Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title></titleInfo><titleInfo type="abbreviated"><title>BBAPRO</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19870724</dateIssued></originInfo><identifier type="ISSN">0167-4838</identifier><identifier type="PII">S0167-4838(00)X0148-3</identifier><part><date>19870724</date><detail type="volume"><number>914</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>103</end></extent><extent unit="pages"><start>19</start><end>27</end></extent></part></relatedItem><identifier type="istex">D13E979A05FA69D0E2DC1CEEAC7EB9421092D418</identifier><identifier type="DOI">10.1016/0167-4838(87)90156-7</identifier><identifier type="PII">0167-4838(87)90156-7</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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