Identification and purification of the 69-kDa intracellular protease involved in the proteolytic processing of the crystal δ-endotoxin of Bacillus thuringiensis subsp. tenebrionis
Abstract The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal δ-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteol...
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| Veröffentlicht in: | FEMS microbiology letters 2000-02, Vol.183 (1), p.63-66 |
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| container_title | FEMS microbiology letters |
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| creator | Reddy, Sreelatha T. Kumar, N. Suresh Venkateswerlu, G. |
| description | Abstract
The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal δ-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteolytic activation of the 73-kDa protoxin indicated the possible role of 69-kDa protease in the proteolytic processing of 73-kDa protoxin. The purified 69-kDa protease was able to cause the proteolytic activation of the 73-kDa protoxin to 68-kDa toxin and this conversion was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline. |
| doi_str_mv | 10.1111/j.1574-6968.2000.tb08934.x |
| format | Article |
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The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal δ-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteolytic activation of the 73-kDa protoxin indicated the possible role of 69-kDa protease in the proteolytic processing of 73-kDa protoxin. The purified 69-kDa protease was able to cause the proteolytic activation of the 73-kDa protoxin to 68-kDa toxin and this conversion was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2000.tb08934.x</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Activation ; Bacillus thuringiensis ; Bacillus thuringiensis subsp. tenebrionis ; Endotoxins ; Ethylenediamine ; Intracellular ; Intracellular protease ; Metalloprotease ; Microbiology ; Protease ; Proteolysis ; Purification ; Toxins ; δ‐Endotoxin</subject><ispartof>FEMS microbiology letters, 2000-02, Vol.183 (1), p.63-66</ispartof><rights>2000 Federation of European Microbiological Societies 2000</rights><rights>2000 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></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.1574-6968.2000.tb08934.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2000.tb08934.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids></links><search><creatorcontrib>Reddy, Sreelatha T.</creatorcontrib><creatorcontrib>Kumar, N. Suresh</creatorcontrib><creatorcontrib>Venkateswerlu, G.</creatorcontrib><title>Identification and purification of the 69-kDa intracellular protease involved in the proteolytic processing of the crystal δ-endotoxin of Bacillus thuringiensis subsp. tenebrionis</title><title>FEMS microbiology letters</title><description>Abstract
The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal δ-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteolytic activation of the 73-kDa protoxin indicated the possible role of 69-kDa protease in the proteolytic processing of 73-kDa protoxin. The purified 69-kDa protease was able to cause the proteolytic activation of the 73-kDa protoxin to 68-kDa toxin and this conversion was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline.</description><subject>Activation</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis subsp. tenebrionis</subject><subject>Endotoxins</subject><subject>Ethylenediamine</subject><subject>Intracellular</subject><subject>Intracellular protease</subject><subject>Metalloprotease</subject><subject>Microbiology</subject><subject>Protease</subject><subject>Proteolysis</subject><subject>Purification</subject><subject>Toxins</subject><subject>δ‐Endotoxin</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp1Uctu3DAMFIoE6GbTfxDSs13J8kuHHpqkeQAb9JK7QNt0qo0ruZKc7P7Xfke_qfJu0lxSXkiQM0MSQ8gZZymP8WWd8qLKk1KWdZoxxtLQsFqKPN18IIt_oyOyYKKqE85k9ZGceL-O0Dxj5YLsbjs0Qfe6haCtoWA6Ok7urWF7Gn4iLWXyeAlUm-CgxWGYBnB0dDYgeIztJzs8YReLPXo_sMM26HauW_Rem4dXrdZtfYCB_tklaDob7Ebv95xDq6Oyj6B4gXnQaLz21E-NH1Ma0GDj4knan5LjHgaPn17yktxffb-_uElWP65vL76tEsuzWiSyw75pMZd93xcF5EyIroq5xQIygKJpiozJLJeSZSC5kKUAYHnR1R3LhRRL8vkgG1_4PaEPam0nZ-JGlQnOWVmVEbckXw-oZz3gVo1O_wK3VZyp2SG1VrMNarZBzQ6pF4fURl3drUoR-cWBb6fxP-zkHbb4Cy9LnRI</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Reddy, Sreelatha T.</creator><creator>Kumar, N. 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The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal δ-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteolytic activation of the 73-kDa protoxin indicated the possible role of 69-kDa protease in the proteolytic processing of 73-kDa protoxin. The purified 69-kDa protease was able to cause the proteolytic activation of the 73-kDa protoxin to 68-kDa toxin and this conversion was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1574-6968.2000.tb08934.x</doi><tpages>4</tpages></addata></record> |
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| ispartof | FEMS microbiology letters, 2000-02, Vol.183 (1), p.63-66 |
| issn | 0378-1097 1574-6968 |
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| source | Oxford University Press Journals All Titles (1996-Current); Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Activation Bacillus thuringiensis Bacillus thuringiensis subsp. tenebrionis Endotoxins Ethylenediamine Intracellular Intracellular protease Metalloprotease Microbiology Protease Proteolysis Purification Toxins δ‐Endotoxin |
| title | Identification and purification of the 69-kDa intracellular protease involved in the proteolytic processing of the crystal δ-endotoxin of Bacillus thuringiensis subsp. tenebrionis |
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