A Cell Plate-Specific Callose Synthase and Its Interaction with Phragmoplastin
Callose is synthesized on the forming cell plate and several other locations in the plant. We cloned an Arabidopsis cDNA encoding a callose synthase (CalS1) catalytic subunit. The CalS1 gene comprises 42 exons with 41 introns and is transcribed into a 6.0-kb mRNA. The deduced peptide, with an approx...
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| Veröffentlicht in: | The Plant cell 2001-04, Vol.13 (4), p.755-768 |
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| creator | Hong, Zonglie Delauney, Ashton J. Desh Pal S. Verma |
| description | Callose is synthesized on the forming cell plate and several other locations in the plant. We cloned an Arabidopsis cDNA encoding a callose synthase (CalS1) catalytic subunit. The CalS1 gene comprises 42 exons with 41 introns and is transcribed into a 6.0-kb mRNA. The deduced peptide, with an approximate molecular mass of 226 kD, showed sequence homology with the yeast 1,3-β-glucan synthases and is distinct from plant cellulose synthases. CalS1 contains 16 predicted transmembrane helices with the N-terminal region and a large central loop facing the cytoplasm. CalS1 interacts with two cell plate-associated proteins, phragmoplastin and a novel UDP-glucose transferase that copurifies with the CalS complex. That CalS1 is a cell plate-specific enzyme is demonstrated by the observations that the green fluorescent protein-CalS1 fusion protein was localized at the growing cell plate, that expression of CalS1 in transgenic tobacco cells enhanced callose synthesis on the forming cell plate, and that these cell lines exhibited higher levels of CalS activity. These data also suggest that plant CalS may form a complex with UDP-glucose transferase to facilitate the transfer of substrate for callose synthesis. |
| doi_str_mv | 10.1105/tpc.13.4.755 |
| format | Article |
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Verma</creator><creatorcontrib>Hong, Zonglie ; Delauney, Ashton J. ; Desh Pal S. Verma</creatorcontrib><description>Callose is synthesized on the forming cell plate and several other locations in the plant. We cloned an Arabidopsis cDNA encoding a callose synthase (CalS1) catalytic subunit. The CalS1 gene comprises 42 exons with 41 introns and is transcribed into a 6.0-kb mRNA. The deduced peptide, with an approximate molecular mass of 226 kD, showed sequence homology with the yeast 1,3-β-glucan synthases and is distinct from plant cellulose synthases. CalS1 contains 16 predicted transmembrane helices with the N-terminal region and a large central loop facing the cytoplasm. CalS1 interacts with two cell plate-associated proteins, phragmoplastin and a novel UDP-glucose transferase that copurifies with the CalS complex. That CalS1 is a cell plate-specific enzyme is demonstrated by the observations that the green fluorescent protein-CalS1 fusion protein was localized at the growing cell plate, that expression of CalS1 in transgenic tobacco cells enhanced callose synthesis on the forming cell plate, and that these cell lines exhibited higher levels of CalS activity. These data also suggest that plant CalS may form a complex with UDP-glucose transferase to facilitate the transfer of substrate for callose synthesis.</description><identifier>ISSN: 1040-4651</identifier><identifier>ISSN: 1532-298X</identifier><identifier>EISSN: 1532-298X</identifier><identifier>DOI: 10.1105/tpc.13.4.755</identifier><identifier>PMID: 11283334</identifier><language>eng</language><publisher>United States: American Society of Plant Physiologists</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Amino acids ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Cell lines ; Cell Wall - metabolism ; Cell walls ; Cells, Cultured ; Cellulose ; Cloning, Molecular ; Complementary DNA ; DNA, Complementary - isolation & purification ; DNA, Plant - isolation & purification ; Enzymes ; Exons ; Glucosyltransferases - genetics ; Glucosyltransferases - metabolism ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Plant cells ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plants ; Plants, Genetically Modified ; Proteins ; Schizosaccharomyces pombe Proteins ; Sequence Analysis, Protein ; Yeasts</subject><ispartof>The Plant cell, 2001-04, Vol.13 (4), p.755-768</ispartof><rights>Copyright 2001 American Society of Plant Physiologists</rights><rights>Copyright American Society of Plant Physiologists Apr 2001</rights><rights>Copyright © 2001, American Society of Plant Physiologists 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c467t-2bf5eda7793e0e1ff98f9f253d1160155b9a6d8a5f4dcb353fe5c3f159356c263</citedby><cites>FETCH-LOGICAL-c467t-2bf5eda7793e0e1ff98f9f253d1160155b9a6d8a5f4dcb353fe5c3f159356c263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3871338$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3871338$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,777,781,800,882,27905,27906,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11283334$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hong, Zonglie</creatorcontrib><creatorcontrib>Delauney, Ashton J.</creatorcontrib><creatorcontrib>Desh Pal S. Verma</creatorcontrib><title>A Cell Plate-Specific Callose Synthase and Its Interaction with Phragmoplastin</title><title>The Plant cell</title><addtitle>Plant Cell</addtitle><description>Callose is synthesized on the forming cell plate and several other locations in the plant. We cloned an Arabidopsis cDNA encoding a callose synthase (CalS1) catalytic subunit. The CalS1 gene comprises 42 exons with 41 introns and is transcribed into a 6.0-kb mRNA. The deduced peptide, with an approximate molecular mass of 226 kD, showed sequence homology with the yeast 1,3-β-glucan synthases and is distinct from plant cellulose synthases. CalS1 contains 16 predicted transmembrane helices with the N-terminal region and a large central loop facing the cytoplasm. CalS1 interacts with two cell plate-associated proteins, phragmoplastin and a novel UDP-glucose transferase that copurifies with the CalS complex. That CalS1 is a cell plate-specific enzyme is demonstrated by the observations that the green fluorescent protein-CalS1 fusion protein was localized at the growing cell plate, that expression of CalS1 in transgenic tobacco cells enhanced callose synthesis on the forming cell plate, and that these cell lines exhibited higher levels of CalS activity. These data also suggest that plant CalS may form a complex with UDP-glucose transferase to facilitate the transfer of substrate for callose synthesis.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Cell lines</subject><subject>Cell Wall - metabolism</subject><subject>Cell walls</subject><subject>Cells, Cultured</subject><subject>Cellulose</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>DNA, Complementary - isolation & purification</subject><subject>DNA, Plant - isolation & purification</subject><subject>Enzymes</subject><subject>Exons</subject><subject>Glucosyltransferases - genetics</subject><subject>Glucosyltransferases - metabolism</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Plant cells</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plants</subject><subject>Plants, Genetically Modified</subject><subject>Proteins</subject><subject>Schizosaccharomyces pombe Proteins</subject><subject>Sequence Analysis, Protein</subject><subject>Yeasts</subject><issn>1040-4651</issn><issn>1532-298X</issn><issn>1532-298X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkU1rGzEQhkVoaT7aW85lKSWnrqPRrFa7hx6CSVpDaAJpoTcha6VYZi1tJbkh_z4KNm3a0wzMM1_vS8gp0BkA5ed50jPAWTMTnB-QI-DIatZ3P1-VnDa0bloOh-Q4pTWlFAT0b8ghAOsQsTki3y6quRnH6nZU2dR3k9HOOl3N1TiGZKq7R59XqiTKD9Uip2rhs4lKZxd89eDyqrpdRXW_CdOoUnb-LXlt1ZjMu308IT-uLr_Pv9bXN18W84vrWjetyDVbWm4GJUSPhhqwtu9sbxnHAaClwPmyV-3QKW6bQS-RozVcowXeI281a_GEfN7NnbbLjRm08TmqUU7RbVR8lEE5-W_Fu5W8D78lIC8Clf6zfX8Mv7YmZblxSRchlDdhm6QQRSpGnxd9-A9ch2305TfJoBNctAIL9GkH6RhSisb-OQSofDZJFpPKatnIYlLB3788_i-8d6UAH3fAOuUQXw5jSIXETgBih0-15Jl1</recordid><startdate>20010401</startdate><enddate>20010401</enddate><creator>Hong, Zonglie</creator><creator>Delauney, Ashton J.</creator><creator>Desh Pal S. 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Verma</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Cell Plate-Specific Callose Synthase and Its Interaction with Phragmoplastin</atitle><jtitle>The Plant cell</jtitle><addtitle>Plant Cell</addtitle><date>2001-04-01</date><risdate>2001</risdate><volume>13</volume><issue>4</issue><spage>755</spage><epage>768</epage><pages>755-768</pages><issn>1040-4651</issn><issn>1532-298X</issn><eissn>1532-298X</eissn><abstract>Callose is synthesized on the forming cell plate and several other locations in the plant. We cloned an Arabidopsis cDNA encoding a callose synthase (CalS1) catalytic subunit. The CalS1 gene comprises 42 exons with 41 introns and is transcribed into a 6.0-kb mRNA. The deduced peptide, with an approximate molecular mass of 226 kD, showed sequence homology with the yeast 1,3-β-glucan synthases and is distinct from plant cellulose synthases. CalS1 contains 16 predicted transmembrane helices with the N-terminal region and a large central loop facing the cytoplasm. CalS1 interacts with two cell plate-associated proteins, phragmoplastin and a novel UDP-glucose transferase that copurifies with the CalS complex. That CalS1 is a cell plate-specific enzyme is demonstrated by the observations that the green fluorescent protein-CalS1 fusion protein was localized at the growing cell plate, that expression of CalS1 in transgenic tobacco cells enhanced callose synthesis on the forming cell plate, and that these cell lines exhibited higher levels of CalS activity. These data also suggest that plant CalS may form a complex with UDP-glucose transferase to facilitate the transfer of substrate for callose synthesis.</abstract><cop>United States</cop><pub>American Society of Plant Physiologists</pub><pmid>11283334</pmid><doi>10.1105/tpc.13.4.755</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current) |
| subjects | Amino Acid Motifs Amino Acid Sequence Amino acids Arabidopsis - genetics Arabidopsis - metabolism Cell lines Cell Wall - metabolism Cell walls Cells, Cultured Cellulose Cloning, Molecular Complementary DNA DNA, Complementary - isolation & purification DNA, Plant - isolation & purification Enzymes Exons Glucosyltransferases - genetics Glucosyltransferases - metabolism Isoenzymes - genetics Isoenzymes - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Molecular Sequence Data Plant cells Plant Proteins - genetics Plant Proteins - metabolism Plants Plants, Genetically Modified Proteins Schizosaccharomyces pombe Proteins Sequence Analysis, Protein Yeasts |
| title | A Cell Plate-Specific Callose Synthase and Its Interaction with Phragmoplastin |
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