Accumulation of pathogenesis‐related (PR) 10/Bet v 1 protein homologues in mulberry (Morus bombycis Koidz.) tree during winter
ABSTRACT Seasonal evaluation of total soluble protein fractions extracted from cortical parenchyma cells of mulberry (Morus bombycis Koidz.) tree identified a predominant 18 kDa protein that was directly correlated to periods of cold acclimation. The 18 kDa protein, designated as WAP18 (winter accum...
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| Veröffentlicht in: | Plant, cell and environment cell and environment, 2004-09, Vol.27 (9), p.1112-1121 |
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| creator | UKAJI, N. KUWABARA, C. TAKEZAWA, D. ARAKAWA, K. FUJIKAWA, S. |
| description | ABSTRACT
Seasonal evaluation of total soluble protein fractions extracted from cortical parenchyma cells of mulberry (Morus bombycis Koidz.) tree identified a predominant 18 kDa protein that was directly correlated to periods of cold acclimation. The 18 kDa protein, designated as WAP18 (winter accumulating 18 kDa proteins) increased from September to December and then gradually decreased until June. The maximum levels of WAP18 were detected in mid‐winter, which corresponds to the maximum freeze tolerance in cortical parenchyma cells of mulberry tree. Two‐dimensional gel electrophoresis confirmed that WAP18 consists of at least three proteins that range between an isoelectric point of 5.0 and 6.0. All three proteins reacted with anti‐WAP18 antibodies, thereby suggesting that they represent individual isoforms. Furthermore, N‐terminal amino acid sequence analysis demonstrated that all three proteins contain high sequence similarity to each other and high homology to pathogenesis‐related (PR) −10/Bet v 1 protein families. The purified WAP18 exhibited in vitro cryoprotective activity for the freeze labile l‐lactate dehydrogenase (LDH) enzyme. These results suggest that WAP18 may function in the freezing tolerance mechanism of cortical parenchyma cells of mulberry tree during winter. |
| doi_str_mv | 10.1111/j.1365-3040.2004.01216.x |
| format | Article |
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Seasonal evaluation of total soluble protein fractions extracted from cortical parenchyma cells of mulberry (Morus bombycis Koidz.) tree identified a predominant 18 kDa protein that was directly correlated to periods of cold acclimation. The 18 kDa protein, designated as WAP18 (winter accumulating 18 kDa proteins) increased from September to December and then gradually decreased until June. The maximum levels of WAP18 were detected in mid‐winter, which corresponds to the maximum freeze tolerance in cortical parenchyma cells of mulberry tree. Two‐dimensional gel electrophoresis confirmed that WAP18 consists of at least three proteins that range between an isoelectric point of 5.0 and 6.0. All three proteins reacted with anti‐WAP18 antibodies, thereby suggesting that they represent individual isoforms. Furthermore, N‐terminal amino acid sequence analysis demonstrated that all three proteins contain high sequence similarity to each other and high homology to pathogenesis‐related (PR) −10/Bet v 1 protein families. The purified WAP18 exhibited in vitro cryoprotective activity for the freeze labile l‐lactate dehydrogenase (LDH) enzyme. These results suggest that WAP18 may function in the freezing tolerance mechanism of cortical parenchyma cells of mulberry tree during winter.</description><identifier>ISSN: 0140-7791</identifier><identifier>EISSN: 1365-3040</identifier><identifier>DOI: 10.1111/j.1365-3040.2004.01216.x</identifier><identifier>CODEN: PLCEDV</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Biological and medical sciences ; Cell biochemistry ; Cell physiology ; cold acclimation ; cryoprotective activity ; freezing tolerance ; Fundamental and applied biological sciences. Psychology ; mulberry tree ; Plant physiology and development ; PR‐10/ Bet v 1 protein family ; soluble protein ; WAP18</subject><ispartof>Plant, cell and environment, 2004-09, Vol.27 (9), p.1112-1121</ispartof><rights>2004 INIST-CNRS</rights><rights>Copyright Blackwell Science Ltd. Sep 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4846-a1e06cfad8d2cf20b6a4df7c7ea5c7292c8045b7ea15cc7c7b5e478953243773</citedby><cites>FETCH-LOGICAL-c4846-a1e06cfad8d2cf20b6a4df7c7ea5c7292c8045b7ea15cc7c7b5e478953243773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-3040.2004.01216.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-3040.2004.01216.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27923,27924,45573,45574,46408,46832</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16083043$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>UKAJI, N.</creatorcontrib><creatorcontrib>KUWABARA, C.</creatorcontrib><creatorcontrib>TAKEZAWA, D.</creatorcontrib><creatorcontrib>ARAKAWA, K.</creatorcontrib><creatorcontrib>FUJIKAWA, S.</creatorcontrib><title>Accumulation of pathogenesis‐related (PR) 10/Bet v 1 protein homologues in mulberry (Morus bombycis Koidz.) tree during winter</title><title>Plant, cell and environment</title><description>ABSTRACT
Seasonal evaluation of total soluble protein fractions extracted from cortical parenchyma cells of mulberry (Morus bombycis Koidz.) tree identified a predominant 18 kDa protein that was directly correlated to periods of cold acclimation. The 18 kDa protein, designated as WAP18 (winter accumulating 18 kDa proteins) increased from September to December and then gradually decreased until June. The maximum levels of WAP18 were detected in mid‐winter, which corresponds to the maximum freeze tolerance in cortical parenchyma cells of mulberry tree. Two‐dimensional gel electrophoresis confirmed that WAP18 consists of at least three proteins that range between an isoelectric point of 5.0 and 6.0. All three proteins reacted with anti‐WAP18 antibodies, thereby suggesting that they represent individual isoforms. Furthermore, N‐terminal amino acid sequence analysis demonstrated that all three proteins contain high sequence similarity to each other and high homology to pathogenesis‐related (PR) −10/Bet v 1 protein families. The purified WAP18 exhibited in vitro cryoprotective activity for the freeze labile l‐lactate dehydrogenase (LDH) enzyme. These results suggest that WAP18 may function in the freezing tolerance mechanism of cortical parenchyma cells of mulberry tree during winter.</description><subject>Biological and medical sciences</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>cold acclimation</subject><subject>cryoprotective activity</subject><subject>freezing tolerance</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>mulberry tree</subject><subject>Plant physiology and development</subject><subject>PR‐10/ Bet v 1 protein family</subject><subject>soluble protein</subject><subject>WAP18</subject><issn>0140-7791</issn><issn>1365-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqNUMtOwzAQtBBIlMc_WEhIcEhqJ46dHjhAVR6iCIS4W46zKa7SuNgJUE58At_Il-BQBFf24n3MzK4HIUxJTEMM5zFNeRalhJE4IYTFhCaUx68baPA72EQDQhmJhBjRbbTj_ZyQ0BCjAXo_1bpbdLVqjW2wrfBStY92Bg144z_fPxyEEZT46O7-OOwcnkGLnzHFS2dbMA1-tAtb21kHHocqCBXg3Aof3VjXeVzYRbHSxuNra8q3-Bi3DgCXnTPNDL-YpgW3h7YqVXvY_3l30cP55GF8GU1vL67Gp9NIs5zxSFEgXFeqzMtEVwkpuGJlJbQAlWmRjBKdE5YVoaSZ1qFfZMBEPsrShKVCpLvoYC0bDn8K17ZybjvXhI0ySTnhgrM8gPI1SDvrvYNKLp1ZKLeSlMjebTmXvamyN1X2bstvt-VroB7-6CuvVV051YR___E5yQMpDbiTNe7F1LD6t768G0_6LP0C4-CT0g</recordid><startdate>200409</startdate><enddate>200409</enddate><creator>UKAJI, N.</creator><creator>KUWABARA, C.</creator><creator>TAKEZAWA, D.</creator><creator>ARAKAWA, K.</creator><creator>FUJIKAWA, S.</creator><general>Blackwell Science Ltd</general><general>Blackwell</general><general>Wiley Subscription Services, Inc</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7ST</scope><scope>C1K</scope><scope>SOI</scope></search><sort><creationdate>200409</creationdate><title>Accumulation of pathogenesis‐related (PR) 10/Bet v 1 protein homologues in mulberry (Morus bombycis Koidz.) tree during winter</title><author>UKAJI, N. ; KUWABARA, C. ; TAKEZAWA, D. ; ARAKAWA, K. ; FUJIKAWA, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4846-a1e06cfad8d2cf20b6a4df7c7ea5c7292c8045b7ea15cc7c7b5e478953243773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Biological and medical sciences</topic><topic>Cell biochemistry</topic><topic>Cell physiology</topic><topic>cold acclimation</topic><topic>cryoprotective activity</topic><topic>freezing tolerance</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>mulberry tree</topic><topic>Plant physiology and development</topic><topic>PR‐10/ Bet v 1 protein family</topic><topic>soluble protein</topic><topic>WAP18</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>UKAJI, N.</creatorcontrib><creatorcontrib>KUWABARA, C.</creatorcontrib><creatorcontrib>TAKEZAWA, D.</creatorcontrib><creatorcontrib>ARAKAWA, K.</creatorcontrib><creatorcontrib>FUJIKAWA, S.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Environment Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Environment Abstracts</collection><jtitle>Plant, cell and environment</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>UKAJI, N.</au><au>KUWABARA, C.</au><au>TAKEZAWA, D.</au><au>ARAKAWA, K.</au><au>FUJIKAWA, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Accumulation of pathogenesis‐related (PR) 10/Bet v 1 protein homologues in mulberry (Morus bombycis Koidz.) tree during winter</atitle><jtitle>Plant, cell and environment</jtitle><date>2004-09</date><risdate>2004</risdate><volume>27</volume><issue>9</issue><spage>1112</spage><epage>1121</epage><pages>1112-1121</pages><issn>0140-7791</issn><eissn>1365-3040</eissn><coden>PLCEDV</coden><abstract>ABSTRACT
Seasonal evaluation of total soluble protein fractions extracted from cortical parenchyma cells of mulberry (Morus bombycis Koidz.) tree identified a predominant 18 kDa protein that was directly correlated to periods of cold acclimation. The 18 kDa protein, designated as WAP18 (winter accumulating 18 kDa proteins) increased from September to December and then gradually decreased until June. The maximum levels of WAP18 were detected in mid‐winter, which corresponds to the maximum freeze tolerance in cortical parenchyma cells of mulberry tree. Two‐dimensional gel electrophoresis confirmed that WAP18 consists of at least three proteins that range between an isoelectric point of 5.0 and 6.0. All three proteins reacted with anti‐WAP18 antibodies, thereby suggesting that they represent individual isoforms. Furthermore, N‐terminal amino acid sequence analysis demonstrated that all three proteins contain high sequence similarity to each other and high homology to pathogenesis‐related (PR) −10/Bet v 1 protein families. The purified WAP18 exhibited in vitro cryoprotective activity for the freeze labile l‐lactate dehydrogenase (LDH) enzyme. These results suggest that WAP18 may function in the freezing tolerance mechanism of cortical parenchyma cells of mulberry tree during winter.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><doi>10.1111/j.1365-3040.2004.01216.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Biological and medical sciences Cell biochemistry Cell physiology cold acclimation cryoprotective activity freezing tolerance Fundamental and applied biological sciences. Psychology mulberry tree Plant physiology and development PR‐10/ Bet v 1 protein family soluble protein WAP18 |
| title | Accumulation of pathogenesis‐related (PR) 10/Bet v 1 protein homologues in mulberry (Morus bombycis Koidz.) tree during winter |
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