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Proteolytic Processing of Class IV Chitinase in the Compatible Interaction of Bean Roots with Fusarium solani
Three chitinase isoenzymes, PvChiE, PvChiF, and PvChiG (molecular masses 29, 28, and 27 kD, respectively), were purified from bean (Phaseolus vulgaris L. cv Saxa) roots infected with the fungal pathogen Fusarium solani f. sp. phaseoli, and their amino acid sequence was partially determined. All sequ...
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| Published in: | Plant physiology (Bethesda) 1996-08, Vol.111 (4), p.1135-1144 |
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| Main Authors: | , , , , |
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| cited_by | cdi_FETCH-LOGICAL-c499t-2b2a54dcd4ab5ecae9120819675a2c87ae4e85221c3161de5a6476ff915fec33 |
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| container_end_page | 1144 |
| container_issue | 4 |
| container_start_page | 1135 |
| container_title | Plant physiology (Bethesda) |
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| creator | Lange, Jürg Mohr, Uwe Wiemken, Andres Boller, Thomas Vögeli-Lange, Regina |
| description | Three chitinase isoenzymes, PvChiE, PvChiF, and PvChiG (molecular masses 29, 28, and 27 kD, respectively), were purified from bean (Phaseolus vulgaris L. cv Saxa) roots infected with the fungal pathogen Fusarium solani f. sp. phaseoli, and their amino acid sequence was partially determined. All sequences from all three isoenzymes exactly matched deduced amino acid sequences of the bean class IV chitinase PvChi4, formerly called PR4. The N terminus of PvChiF mapped to the hinge region, and the N terminus of PvChiG mapped to the catalytic domain of PvChi4. The N terminus of PvChiE was blocked. The appearance of PvChiE, PvChiF, and PvChiG correlated with an increase in protease activity in infected roots, and they could be generated in vitro by mixing extracts with high protease activity with extracts containing high amounts of PvChi4. Extracts from infected roots prepared in the presence of protease inhibitors also contained the processed forms of PvChi4, indicating that processing occurred in planta and not as an artifact of extraction. Processing of PvChi4 was not detected in incompatible interactions with a nonhost strain of F. solani and in symbiotic interactions with Glomus mosseae, and thus may be important only in compatible interactions with F. solani. |
| doi_str_mv | 10.1104/pp.111.4.1135 |
| format | article |
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All sequences from all three isoenzymes exactly matched deduced amino acid sequences of the bean class IV chitinase PvChi4, formerly called PR4. The N terminus of PvChiF mapped to the hinge region, and the N terminus of PvChiG mapped to the catalytic domain of PvChi4. The N terminus of PvChiE was blocked. The appearance of PvChiE, PvChiF, and PvChiG correlated with an increase in protease activity in infected roots, and they could be generated in vitro by mixing extracts with high protease activity with extracts containing high amounts of PvChi4. Extracts from infected roots prepared in the presence of protease inhibitors also contained the processed forms of PvChi4, indicating that processing occurred in planta and not as an artifact of extraction. Processing of PvChi4 was not detected in incompatible interactions with a nonhost strain of F. solani and in symbiotic interactions with Glomus mosseae, and thus may be important only in compatible interactions with F. solani.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.111.4.1135</identifier><identifier>PMID: 8756497</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>Amino Acid Sequence ; Amino acids ; Biological and medical sciences ; Chitinases - biosynthesis ; Chitinases - chemistry ; Chitinases - metabolism ; Chlorides ; Enzyme Induction ; Enzymes ; Fabaceae - microbiology ; Fundamental and applied biological sciences. Psychology ; Fungal plant pathogens ; Fungi ; Fusarium - pathogenicity ; Gels ; Humans ; Hydrolysis ; Isoenzymes - biosynthesis ; Isoenzymes - chemistry ; Isoenzymes - metabolism ; Molecular Sequence Data ; Mosses ; Pathogens ; Pathology, epidemiology, host-fungus relationships. Damages, economic importance ; Phytopathology. Animal pests. Plant and forest protection ; Plant roots ; Plant Roots - microbiology ; Plant-Microbe and Plant-Insect Interactions ; Plants ; Plants, Medicinal ; Protein Processing, Post-Translational ; Proteins ; Sequence Homology, Amino Acid</subject><ispartof>Plant physiology (Bethesda), 1996-08, Vol.111 (4), p.1135-1144</ispartof><rights>Copyright 1996 American Society of Plant Physiologists</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-2b2a54dcd4ab5ecae9120819675a2c87ae4e85221c3161de5a6476ff915fec33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4277266$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4277266$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,786,790,891,27957,27958,58593,58826</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3190735$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8756497$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lange, Jürg</creatorcontrib><creatorcontrib>Mohr, Uwe</creatorcontrib><creatorcontrib>Wiemken, Andres</creatorcontrib><creatorcontrib>Boller, Thomas</creatorcontrib><creatorcontrib>Vögeli-Lange, Regina</creatorcontrib><title>Proteolytic Processing of Class IV Chitinase in the Compatible Interaction of Bean Roots with Fusarium solani</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Three chitinase isoenzymes, PvChiE, PvChiF, and PvChiG (molecular masses 29, 28, and 27 kD, respectively), were purified from bean (Phaseolus vulgaris L. cv Saxa) roots infected with the fungal pathogen Fusarium solani f. sp. phaseoli, and their amino acid sequence was partially determined. All sequences from all three isoenzymes exactly matched deduced amino acid sequences of the bean class IV chitinase PvChi4, formerly called PR4. The N terminus of PvChiF mapped to the hinge region, and the N terminus of PvChiG mapped to the catalytic domain of PvChi4. The N terminus of PvChiE was blocked. The appearance of PvChiE, PvChiF, and PvChiG correlated with an increase in protease activity in infected roots, and they could be generated in vitro by mixing extracts with high protease activity with extracts containing high amounts of PvChi4. Extracts from infected roots prepared in the presence of protease inhibitors also contained the processed forms of PvChi4, indicating that processing occurred in planta and not as an artifact of extraction. Processing of PvChi4 was not detected in incompatible interactions with a nonhost strain of F. solani and in symbiotic interactions with Glomus mosseae, and thus may be important only in compatible interactions with F. solani.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Biological and medical sciences</subject><subject>Chitinases - biosynthesis</subject><subject>Chitinases - chemistry</subject><subject>Chitinases - metabolism</subject><subject>Chlorides</subject><subject>Enzyme Induction</subject><subject>Enzymes</subject><subject>Fabaceae - microbiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal plant pathogens</subject><subject>Fungi</subject><subject>Fusarium - pathogenicity</subject><subject>Gels</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Isoenzymes - biosynthesis</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mosses</subject><subject>Pathogens</subject><subject>Pathology, epidemiology, host-fungus relationships. Damages, economic importance</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Plant roots</subject><subject>Plant Roots - microbiology</subject><subject>Plant-Microbe and Plant-Insect Interactions</subject><subject>Plants</subject><subject>Plants, Medicinal</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Sequence Homology, Amino Acid</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqFkcFrFDEUxoModa0evSnkIL1NTTJJJjl4qEOrCwVFiteQzb7ppswkY5JR-t-bdZdFT17yPfh-3yOPD6HXlFxSSvj7ea5KL3l9W_EErahoWcMEV0_RipA6E6X0c_Qi5wdCCG0pP0NnqhOS626Fpq8pFojjY_EO19lBzj7c4zjgfrQ54_V33O988cFmwD7gsgPcx2m2xW9GwOtQIFlXfAz7zEewAX-LsWT8y5cdvlmyTX6ZcI6jDf4lejbYMcOro56ju5vru_5zc_vl07q_um0c17o0bMOs4Fu35XYjwFnQlBFFteyEZU51FjgowRh1LZV0C8JK3slh0FQM4Nr2HH04rJ2XzQRbB6EkO5o5-cmmRxOtN_86we_MffxpqCRa6Zq_OOZT_LFALmby2cFYT4C4ZNMpxjUT9L8glUwSJWQFmwPoUsw5wXD6DCVmX6OZ56rUcLOvsfJv_77gRB97q_67o2-zs-OQbHA-n7CWatL9WfPmgD3kEtPJ5qzrmJTtb8sdsMI</recordid><startdate>19960801</startdate><enddate>19960801</enddate><creator>Lange, Jürg</creator><creator>Mohr, Uwe</creator><creator>Wiemken, Andres</creator><creator>Boller, Thomas</creator><creator>Vögeli-Lange, Regina</creator><general>American Society of Plant Physiologists</general><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>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19960801</creationdate><title>Proteolytic Processing of Class IV Chitinase in the Compatible Interaction of Bean Roots with Fusarium solani</title><author>Lange, Jürg ; Mohr, Uwe ; Wiemken, Andres ; Boller, Thomas ; Vögeli-Lange, Regina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-2b2a54dcd4ab5ecae9120819675a2c87ae4e85221c3161de5a6476ff915fec33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Biological and medical sciences</topic><topic>Chitinases - biosynthesis</topic><topic>Chitinases - chemistry</topic><topic>Chitinases - metabolism</topic><topic>Chlorides</topic><topic>Enzyme Induction</topic><topic>Enzymes</topic><topic>Fabaceae - microbiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal plant pathogens</topic><topic>Fungi</topic><topic>Fusarium - pathogenicity</topic><topic>Gels</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Isoenzymes - biosynthesis</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mosses</topic><topic>Pathogens</topic><topic>Pathology, epidemiology, host-fungus relationships. Damages, economic importance</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Plant roots</topic><topic>Plant Roots - microbiology</topic><topic>Plant-Microbe and Plant-Insect Interactions</topic><topic>Plants</topic><topic>Plants, Medicinal</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lange, Jürg</creatorcontrib><creatorcontrib>Mohr, Uwe</creatorcontrib><creatorcontrib>Wiemken, Andres</creatorcontrib><creatorcontrib>Boller, Thomas</creatorcontrib><creatorcontrib>Vögeli-Lange, Regina</creatorcontrib><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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lange, Jürg</au><au>Mohr, Uwe</au><au>Wiemken, Andres</au><au>Boller, Thomas</au><au>Vögeli-Lange, Regina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteolytic Processing of Class IV Chitinase in the Compatible Interaction of Bean Roots with Fusarium solani</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1996-08-01</date><risdate>1996</risdate><volume>111</volume><issue>4</issue><spage>1135</spage><epage>1144</epage><pages>1135-1144</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><notes>ObjectType-Article-1</notes><notes>ObjectType-Feature-2</notes><abstract>Three chitinase isoenzymes, PvChiE, PvChiF, and PvChiG (molecular masses 29, 28, and 27 kD, respectively), were purified from bean (Phaseolus vulgaris L. cv Saxa) roots infected with the fungal pathogen Fusarium solani f. sp. phaseoli, and their amino acid sequence was partially determined. All sequences from all three isoenzymes exactly matched deduced amino acid sequences of the bean class IV chitinase PvChi4, formerly called PR4. The N terminus of PvChiF mapped to the hinge region, and the N terminus of PvChiG mapped to the catalytic domain of PvChi4. The N terminus of PvChiE was blocked. The appearance of PvChiE, PvChiF, and PvChiG correlated with an increase in protease activity in infected roots, and they could be generated in vitro by mixing extracts with high protease activity with extracts containing high amounts of PvChi4. Extracts from infected roots prepared in the presence of protease inhibitors also contained the processed forms of PvChi4, indicating that processing occurred in planta and not as an artifact of extraction. Processing of PvChi4 was not detected in incompatible interactions with a nonhost strain of F. solani and in symbiotic interactions with Glomus mosseae, and thus may be important only in compatible interactions with F. solani.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>8756497</pmid><doi>10.1104/pp.111.4.1135</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0032-0889 |
| ispartof | Plant physiology (Bethesda), 1996-08, Vol.111 (4), p.1135-1144 |
| issn | 0032-0889 1532-2548 |
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| source | JSTOR Archival Journals and Primary Sources Collection; OUP_牛津大学出版社现刊 |
| subjects | Amino Acid Sequence Amino acids Biological and medical sciences Chitinases - biosynthesis Chitinases - chemistry Chitinases - metabolism Chlorides Enzyme Induction Enzymes Fabaceae - microbiology Fundamental and applied biological sciences. Psychology Fungal plant pathogens Fungi Fusarium - pathogenicity Gels Humans Hydrolysis Isoenzymes - biosynthesis Isoenzymes - chemistry Isoenzymes - metabolism Molecular Sequence Data Mosses Pathogens Pathology, epidemiology, host-fungus relationships. Damages, economic importance Phytopathology. Animal pests. Plant and forest protection Plant roots Plant Roots - microbiology Plant-Microbe and Plant-Insect Interactions Plants Plants, Medicinal Protein Processing, Post-Translational Proteins Sequence Homology, Amino Acid |
| title | Proteolytic Processing of Class IV Chitinase in the Compatible Interaction of Bean Roots with Fusarium solani |
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