Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki
The gene encoding the 66-kDa entomocidal protein (P2 protein or mosquito factor) from Bacillus thuringiensis var. kurstaki has been isolated by the use of a 62-mer oligonucleotide probe that encoded 21 amino acids of the P2 protein NH2 terminus. The DNA sequence of the gene, designated cryBI, was un...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1988-01, Vol.263 (1), p.561-567 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 567 |
|---|---|
| container_issue | 1 |
| container_start_page | 561 |
| container_title | The Journal of biological chemistry |
| container_volume | 263 |
| creator | Donovan, W P Dankocsik, C C Gilbert, M P Gawron-Burke, M C Groat, R G Carlton, B C |
| description | The gene encoding the 66-kDa entomocidal protein (P2 protein or mosquito factor) from Bacillus thuringiensis var. kurstaki has been isolated by the use of a 62-mer oligonucleotide probe that encoded 21 amino acids of the P2 protein NH2 terminus. The DNA sequence of the gene, designated cryBI, was unique from the published sequences of other B. thuringiensis genes. However, the amino acid sequence of the P2 protein, as deduced from the DNA sequence of the cryBI gene, was found to contain a sequence of 100 amino acids having 37% homology to a group of B. thuringiensis entomocidal proteins, the P1 proteins. Late stationary phase Bacillus megaterium cells harboring the cloned B. thuringiensis cryBI gene contained large aggregates of the P2 protein, and the cells were highly toxic to both lepidopteran and dipteran larvae. In contrast, Escherichia coli cells harboring the cloned cryBI gene contained very low levels of the P2 protein. DNA blot hybridization experiments showed that certain B. thuringiensis strains contained at least one cryBI-related DNA sequence in addition to the cryBI gene itself. |
| doi_str_mv | 10.1016/S0021-9258(19)57428-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_14844167</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925819574282</els_id><sourcerecordid>14844167</sourcerecordid><originalsourceid>FETCH-LOGICAL-c493t-d64091b841ddab2700c59fa198457951a61ec9a843322c42d01ac5a6d3c71ec03</originalsourceid><addsrcrecordid>eNqFkUuLFDEUhYMoYzv6EwYiiOii2txUUo-VtIMvGFBQwV1IJ6np61QlM0mqtZf-c9PTTW_NJpDznfs4IeQC2BIYNG--Mcah6rnsXkH_WraCdxV_QBbAurqqJfx8SBYn5DF5ktIvVo7o4Yyc1cChAbkgf1cT-kC1QUuTu5udN45qb6nzOUyhPOuxqBm3mHc0DDRvHP3KqYm7lIt0G0N26Jd05Sn65EymOfxBT4cYJvqu1B3HORXXHNFfo_MJE93quKQ3cywVbvApeTToMblnx_uc_Pjw_vvlp-rqy8fPl6uryoi-zpVtBOth3QmwVq95y5iR_aCh74Rsewm6AWd63Ym65twIbhloI3Vja9MWhdXn5OWhbhm57JmymjAZN47auzAnBaITApq2gPIAmhhSim5QtxEnHXcKmNpHr-6jV_tcFfTqPnrFi-_i2GBeT86eXMesi_7iqOtk9DhE7Q2mE9aWlVq-x54fsA1eb35jdGqNwWzcpHhTK1CygcK8PTCuBLZFF1UyuP86W3iTlQ34n2H_AchFrCY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14844167</pqid></control><display><type>article</type><title>Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Donovan, W P ; Dankocsik, C C ; Gilbert, M P ; Gawron-Burke, M C ; Groat, R G ; Carlton, B C</creator><creatorcontrib>Donovan, W P ; Dankocsik, C C ; Gilbert, M P ; Gawron-Burke, M C ; Groat, R G ; Carlton, B C</creatorcontrib><description>The gene encoding the 66-kDa entomocidal protein (P2 protein or mosquito factor) from Bacillus thuringiensis var. kurstaki has been isolated by the use of a 62-mer oligonucleotide probe that encoded 21 amino acids of the P2 protein NH2 terminus. The DNA sequence of the gene, designated cryBI, was unique from the published sequences of other B. thuringiensis genes. However, the amino acid sequence of the P2 protein, as deduced from the DNA sequence of the cryBI gene, was found to contain a sequence of 100 amino acids having 37% homology to a group of B. thuringiensis entomocidal proteins, the P1 proteins. Late stationary phase Bacillus megaterium cells harboring the cloned B. thuringiensis cryBI gene contained large aggregates of the P2 protein, and the cells were highly toxic to both lepidopteran and dipteran larvae. In contrast, Escherichia coli cells harboring the cloned cryBI gene contained very low levels of the P2 protein. DNA blot hybridization experiments showed that certain B. thuringiensis strains contained at least one cryBI-related DNA sequence in addition to the cryBI gene itself.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)57428-2</identifier><identifier>PMID: 3121615</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Bacillus megaterium - genetics ; Bacillus thuringiensis ; Bacillus thuringiensis - genetics ; Bacillus thuringiensis kurstaki ; Bacterial Toxins - genetics ; Bacterial Toxins - pharmacology ; Base Sequence ; Biological and medical sciences ; cloning ; Cloning, Molecular ; Diptera ; Diptera - drug effects ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; gene expression ; Genes ; Genes, Bacterial ; Holoproteins ; Insecticides ; Larva ; Lepidoptera ; Lepidoptera - drug effects ; Molecular Sequence Data ; Other proteins ; Protein Precursors - genetics ; Protein Precursors - pharmacology ; Proteins ; spore crystals</subject><ispartof>The Journal of biological chemistry, 1988-01, Vol.263 (1), p.561-567</ispartof><rights>1988 © 1988 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c493t-d64091b841ddab2700c59fa198457951a61ec9a843322c42d01ac5a6d3c71ec03</citedby><cites>FETCH-LOGICAL-c493t-d64091b841ddab2700c59fa198457951a61ec9a843322c42d01ac5a6d3c71ec03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7700725$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3121615$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Donovan, W P</creatorcontrib><creatorcontrib>Dankocsik, C C</creatorcontrib><creatorcontrib>Gilbert, M P</creatorcontrib><creatorcontrib>Gawron-Burke, M C</creatorcontrib><creatorcontrib>Groat, R G</creatorcontrib><creatorcontrib>Carlton, B C</creatorcontrib><title>Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The gene encoding the 66-kDa entomocidal protein (P2 protein or mosquito factor) from Bacillus thuringiensis var. kurstaki has been isolated by the use of a 62-mer oligonucleotide probe that encoded 21 amino acids of the P2 protein NH2 terminus. The DNA sequence of the gene, designated cryBI, was unique from the published sequences of other B. thuringiensis genes. However, the amino acid sequence of the P2 protein, as deduced from the DNA sequence of the cryBI gene, was found to contain a sequence of 100 amino acids having 37% homology to a group of B. thuringiensis entomocidal proteins, the P1 proteins. Late stationary phase Bacillus megaterium cells harboring the cloned B. thuringiensis cryBI gene contained large aggregates of the P2 protein, and the cells were highly toxic to both lepidopteran and dipteran larvae. In contrast, Escherichia coli cells harboring the cloned cryBI gene contained very low levels of the P2 protein. DNA blot hybridization experiments showed that certain B. thuringiensis strains contained at least one cryBI-related DNA sequence in addition to the cryBI gene itself.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Bacillus megaterium - genetics</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - genetics</subject><subject>Bacillus thuringiensis kurstaki</subject><subject>Bacterial Toxins - genetics</subject><subject>Bacterial Toxins - pharmacology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>cloning</subject><subject>Cloning, Molecular</subject><subject>Diptera</subject><subject>Diptera - drug effects</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene expression</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>Holoproteins</subject><subject>Insecticides</subject><subject>Larva</subject><subject>Lepidoptera</subject><subject>Lepidoptera - drug effects</subject><subject>Molecular Sequence Data</subject><subject>Other proteins</subject><subject>Protein Precursors - genetics</subject><subject>Protein Precursors - pharmacology</subject><subject>Proteins</subject><subject>spore crystals</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEUhYMoYzv6EwYiiOii2txUUo-VtIMvGFBQwV1IJ6np61QlM0mqtZf-c9PTTW_NJpDznfs4IeQC2BIYNG--Mcah6rnsXkH_WraCdxV_QBbAurqqJfx8SBYn5DF5ktIvVo7o4Yyc1cChAbkgf1cT-kC1QUuTu5udN45qb6nzOUyhPOuxqBm3mHc0DDRvHP3KqYm7lIt0G0N26Jd05Sn65EymOfxBT4cYJvqu1B3HORXXHNFfo_MJE93quKQ3cywVbvApeTToMblnx_uc_Pjw_vvlp-rqy8fPl6uryoi-zpVtBOth3QmwVq95y5iR_aCh74Rsewm6AWd63Ym65twIbhloI3Vja9MWhdXn5OWhbhm57JmymjAZN47auzAnBaITApq2gPIAmhhSim5QtxEnHXcKmNpHr-6jV_tcFfTqPnrFi-_i2GBeT86eXMesi_7iqOtk9DhE7Q2mE9aWlVq-x54fsA1eb35jdGqNwWzcpHhTK1CygcK8PTCuBLZFF1UyuP86W3iTlQ34n2H_AchFrCY</recordid><startdate>19880105</startdate><enddate>19880105</enddate><creator>Donovan, W P</creator><creator>Dankocsik, C C</creator><creator>Gilbert, M P</creator><creator>Gawron-Burke, M C</creator><creator>Groat, R G</creator><creator>Carlton, B C</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19880105</creationdate><title>Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki</title><author>Donovan, W P ; Dankocsik, C C ; Gilbert, M P ; Gawron-Burke, M C ; Groat, R G ; Carlton, B C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c493t-d64091b841ddab2700c59fa198457951a61ec9a843322c42d01ac5a6d3c71ec03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Bacillus megaterium - genetics</topic><topic>Bacillus thuringiensis</topic><topic>Bacillus thuringiensis - genetics</topic><topic>Bacillus thuringiensis kurstaki</topic><topic>Bacterial Toxins - genetics</topic><topic>Bacterial Toxins - pharmacology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>cloning</topic><topic>Cloning, Molecular</topic><topic>Diptera</topic><topic>Diptera - drug effects</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene expression</topic><topic>Genes</topic><topic>Genes, Bacterial</topic><topic>Holoproteins</topic><topic>Insecticides</topic><topic>Larva</topic><topic>Lepidoptera</topic><topic>Lepidoptera - drug effects</topic><topic>Molecular Sequence Data</topic><topic>Other proteins</topic><topic>Protein Precursors - genetics</topic><topic>Protein Precursors - pharmacology</topic><topic>Proteins</topic><topic>spore crystals</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Donovan, W P</creatorcontrib><creatorcontrib>Dankocsik, C C</creatorcontrib><creatorcontrib>Gilbert, M P</creatorcontrib><creatorcontrib>Gawron-Burke, M C</creatorcontrib><creatorcontrib>Groat, R G</creatorcontrib><creatorcontrib>Carlton, B C</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Donovan, W P</au><au>Dankocsik, C C</au><au>Gilbert, M P</au><au>Gawron-Burke, M C</au><au>Groat, R G</au><au>Carlton, B C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-01-05</date><risdate>1988</risdate><volume>263</volume><issue>1</issue><spage>561</spage><epage>567</epage><pages>561-567</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The gene encoding the 66-kDa entomocidal protein (P2 protein or mosquito factor) from Bacillus thuringiensis var. kurstaki has been isolated by the use of a 62-mer oligonucleotide probe that encoded 21 amino acids of the P2 protein NH2 terminus. The DNA sequence of the gene, designated cryBI, was unique from the published sequences of other B. thuringiensis genes. However, the amino acid sequence of the P2 protein, as deduced from the DNA sequence of the cryBI gene, was found to contain a sequence of 100 amino acids having 37% homology to a group of B. thuringiensis entomocidal proteins, the P1 proteins. Late stationary phase Bacillus megaterium cells harboring the cloned B. thuringiensis cryBI gene contained large aggregates of the P2 protein, and the cells were highly toxic to both lepidopteran and dipteran larvae. In contrast, Escherichia coli cells harboring the cloned cryBI gene contained very low levels of the P2 protein. DNA blot hybridization experiments showed that certain B. thuringiensis strains contained at least one cryBI-related DNA sequence in addition to the cryBI gene itself.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3121615</pmid><doi>10.1016/S0021-9258(19)57428-2</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1988-01, Vol.263 (1), p.561-567 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_14844167 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Bacillus megaterium - genetics Bacillus thuringiensis Bacillus thuringiensis - genetics Bacillus thuringiensis kurstaki Bacterial Toxins - genetics Bacterial Toxins - pharmacology Base Sequence Biological and medical sciences cloning Cloning, Molecular Diptera Diptera - drug effects Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gene expression Genes Genes, Bacterial Holoproteins Insecticides Larva Lepidoptera Lepidoptera - drug effects Molecular Sequence Data Other proteins Protein Precursors - genetics Protein Precursors - pharmacology Proteins spore crystals |
| title | Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T03%3A34%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amino%20acid%20sequence%20and%20entomocidal%20activity%20of%20the%20P2%20crystal%20protein.%20An%20insect%20toxin%20from%20Bacillus%20thuringiensis%20var.%20kurstaki&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Donovan,%20W%20P&rft.date=1988-01-05&rft.volume=263&rft.issue=1&rft.spage=561&rft.epage=567&rft.pages=561-567&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(19)57428-2&rft_dat=%3Cproquest_cross%3E14844167%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14844167&rft_id=info:pmid/3121615&rft_els_id=S0021925819574282&rfr_iscdi=true |