A Specific α-Tubulin is Associated with the Initiation of Parthenogenesis in 'Salmon' Wheat Lines
The ‘Salmon system’ consists of isogenic but alloplasmic wheat lines with either sexual or autonomous embryo development. Using two‐dimensional gel electrophoresis these lines have been screened for proteins potentially involved in the initiation of parthenogenesis. A temporally altered expression o...
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Veröffentlicht in: | Hereditas 1997-01, Vol.126 (3), p.219-224 |
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creator | Matzk, Fritz Meyer, Hans-Martin Horstmann, Christian Balzer, Hans-Jörg Bäumlein, Helmut Schubert, Ingo |
description | The ‘Salmon system’ consists of isogenic but alloplasmic wheat lines with either sexual or autonomous embryo development. Using two‐dimensional gel electrophoresis these lines have been screened for proteins potentially involved in the initiation of parthenogenesis. A temporally altered expression of the polypeptide ‘P 115.1’ in the sexual and parthenogenetic ‘Salmon’ lines seems to be related with the autonomous embryo formation. Around anthesis when most of the egg cells begin the parthenogenetic development, the polypeptide ‘P 115.1’ was present in ovaries of the parthenogenetic lines but not in ovaries of the sexual line. Moreover, this polypeptide is only expressed in the ovaries of amphidiploid parthenogenetic plants containing differentiated embryo sacs. It is absent from ovaries of the analogous polyhaploid plants, which lack any embryo sac structure within their ovules. Furthermore, the polypeptide was neither detectable in meristematic tissue of root tips nor in leaves. N‐terminal amino acid sequencing identified ‘P 115.1’ as an α‐tubulin. Thus, ‘P 115.1’ apparently represents an embryo sac‐specific isoform of α‐tubulin involved in the initiation of embryo development. |
doi_str_mv | 10.1111/j.1601-5223.1997.00219.x |
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Using two‐dimensional gel electrophoresis these lines have been screened for proteins potentially involved in the initiation of parthenogenesis. A temporally altered expression of the polypeptide ‘P 115.1’ in the sexual and parthenogenetic ‘Salmon’ lines seems to be related with the autonomous embryo formation. Around anthesis when most of the egg cells begin the parthenogenetic development, the polypeptide ‘P 115.1’ was present in ovaries of the parthenogenetic lines but not in ovaries of the sexual line. Moreover, this polypeptide is only expressed in the ovaries of amphidiploid parthenogenetic plants containing differentiated embryo sacs. It is absent from ovaries of the analogous polyhaploid plants, which lack any embryo sac structure within their ovules. Furthermore, the polypeptide was neither detectable in meristematic tissue of root tips nor in leaves. N‐terminal amino acid sequencing identified ‘P 115.1’ as an α‐tubulin. Thus, ‘P 115.1’ apparently represents an embryo sac‐specific isoform of α‐tubulin involved in the initiation of embryo development.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis - genetics</subject><subject>Parthenogenesis</subject><subject>Sequence Alignment</subject><subject>Triticum - genetics</subject><subject>Triticum - physiology</subject><subject>Triticum aestivum</subject><subject>Tubulin - biosynthesis</subject><subject>Tubulin - chemistry</subject><issn>0018-0661</issn><issn>1601-5223</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1DAUha0KVIa2j4DkFV0l2HFixwsWowKdiqhUtFWXln9uGA-ZZBon6vSx-iJ9JhxmNFvwwj_3nO9aOhchTElK4_q0SiknNCmyjKVUSpESklGZbo_Q7CC8QTNCaJkQzuk79D6EVXwKSdkxOpasIJTxGTJzfLsB62tv8etLcjeasfEt9gHPQ-is1wM4_OSHJR6WgK9aP8SS71rc1fhG97HYdr-ghRCJyJ3f6mbdtef4YQl6wJWPyil6W-smwNn-PEH3377eXSyS6sfl1cW8SmzOmEw0EYY4LXUmhTEGXG6csY6VOThwRTHtruZ5DlYYltfgiChKS4Uutc2FYyfo467vpu8eRwiDWvtgoWl0C90YlJCMy6Is_mmMCUpe8jway53R9l0IPdRq0_u17p8VJWqag1pNZqqmuNU0B_V3Dmob0Q_7P0azBncA98FH_fNOf_INPP93X7X4-SWLt8gnO96HAbYHXve_FRdMFOrh-lJVVXkjrhffFWd_AG-Pp5c</recordid><startdate>19970101</startdate><enddate>19970101</enddate><creator>Matzk, Fritz</creator><creator>Meyer, Hans-Martin</creator><creator>Horstmann, Christian</creator><creator>Balzer, Hans-Jörg</creator><creator>Bäumlein, Helmut</creator><creator>Schubert, Ingo</creator><general>Munksgaard International Publishers</general><scope>BSCLL</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19970101</creationdate><title>A Specific α-Tubulin is Associated with the Initiation of Parthenogenesis in 'Salmon' Wheat Lines</title><author>Matzk, Fritz ; Meyer, Hans-Martin ; Horstmann, Christian ; Balzer, Hans-Jörg ; Bäumlein, Helmut ; Schubert, Ingo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4339-a07b0da9a297bbbed4bdbcd384eded55ededdf644ec7b34fed0758c17a8ac47d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis - genetics</topic><topic>Parthenogenesis</topic><topic>Sequence Alignment</topic><topic>Triticum - genetics</topic><topic>Triticum - physiology</topic><topic>Triticum aestivum</topic><topic>Tubulin - biosynthesis</topic><topic>Tubulin - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matzk, Fritz</creatorcontrib><creatorcontrib>Meyer, Hans-Martin</creatorcontrib><creatorcontrib>Horstmann, Christian</creatorcontrib><creatorcontrib>Balzer, Hans-Jörg</creatorcontrib><creatorcontrib>Bäumlein, Helmut</creatorcontrib><creatorcontrib>Schubert, Ingo</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Hereditas</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Matzk, Fritz</au><au>Meyer, Hans-Martin</au><au>Horstmann, Christian</au><au>Balzer, Hans-Jörg</au><au>Bäumlein, Helmut</au><au>Schubert, Ingo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Specific α-Tubulin is Associated with the Initiation of Parthenogenesis in 'Salmon' Wheat Lines</atitle><jtitle>Hereditas</jtitle><addtitle>Hereditas</addtitle><date>1997-01-01</date><risdate>1997</risdate><volume>126</volume><issue>3</issue><spage>219</spage><epage>224</epage><pages>219-224</pages><issn>0018-0661</issn><eissn>1601-5223</eissn><abstract>The ‘Salmon system’ consists of isogenic but alloplasmic wheat lines with either sexual or autonomous embryo development. Using two‐dimensional gel electrophoresis these lines have been screened for proteins potentially involved in the initiation of parthenogenesis. A temporally altered expression of the polypeptide ‘P 115.1’ in the sexual and parthenogenetic ‘Salmon’ lines seems to be related with the autonomous embryo formation. Around anthesis when most of the egg cells begin the parthenogenetic development, the polypeptide ‘P 115.1’ was present in ovaries of the parthenogenetic lines but not in ovaries of the sexual line. Moreover, this polypeptide is only expressed in the ovaries of amphidiploid parthenogenetic plants containing differentiated embryo sacs. It is absent from ovaries of the analogous polyhaploid plants, which lack any embryo sac structure within their ovules. Furthermore, the polypeptide was neither detectable in meristematic tissue of root tips nor in leaves. N‐terminal amino acid sequencing identified ‘P 115.1’ as an α‐tubulin. Thus, ‘P 115.1’ apparently represents an embryo sac‐specific isoform of α‐tubulin involved in the initiation of embryo development.</abstract><cop>Oxford, UK</cop><pub>Munksgaard International Publishers</pub><pmid>9350136</pmid><doi>10.1111/j.1601-5223.1997.00219.x</doi><tpages>6</tpages></addata></record> |
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subjects | Amino Acid Sequence Arabidopsis - genetics Parthenogenesis Sequence Alignment Triticum - genetics Triticum - physiology Triticum aestivum Tubulin - biosynthesis Tubulin - chemistry |
title | A Specific α-Tubulin is Associated with the Initiation of Parthenogenesis in 'Salmon' Wheat Lines |
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