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The three β-1,3-glucanases from Acremonium blochii strain C59 appear to be encoded by separate genes
Three exocellular β-1,3-glucanases from Acremonium blochii strain C59, BGN3.2, BGN3.3 and BGN3.4, were purified. Two, BGN3.2 and BGN3.4 appeared to act as exo-enzymes against laminarin from Laminaria digitata, while BGN3.3 displayed an endo-mode of action. The N-terminal amino acid sequence data for...
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Published in: | Mycological research 2006, Vol.110 (1), p.66-74 |
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creator | Martin, Kirstee L. McDougall, Barbara M. Unkles, Shiela E. Seviour, Robert J. |
description | Three exocellular β-1,3-glucanases from
Acremonium blochii strain C59, BGN3.2, BGN3.3 and BGN3.4, were purified. Two, BGN3.2 and BGN3.4 appeared to act as exo-enzymes against laminarin from
Laminaria digitata, while BGN3.3 displayed an endo-mode of action. The N-terminal amino acid sequence data for BGN3.2 and BGN3.4 suggested these two enzymes may be encoded by different genes. The gene encoding the BGN3.2 glucanase was fully sequenced, and its deduced amino acid sequence was similar to those for all other sequenced fungal exo-β-1,3-glucanases. This
BGN3.2 gene consists of an uninterrupted ORF of 2349
bp encoding 783 amino acids possibly with two cleavage sites for the potential removal of a pre- and pro-protein, respectively. A DNA fragment encoding a portion of the
BGN3.4 gene was amplified by PCR, and the nucleotide sequence of this fragment confirmed that BGN3.2 and BGN3.4 are encoded by different genes. The internal peptide sequences of BGN3.3 were not present in the amino acid sequence deduced from the
BGN3.2 gene, reinforcing the view that BGN3.3 is also genetically different to BGN3.2. Genetic differences between multiple forms of fungal β-1,3-glucanases from a single fungus have not been reported previously. |
doi_str_mv | 10.1016/j.mycres.2005.08.004 |
format | article |
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Acremonium blochii strain C59, BGN3.2, BGN3.3 and BGN3.4, were purified. Two, BGN3.2 and BGN3.4 appeared to act as exo-enzymes against laminarin from
Laminaria digitata, while BGN3.3 displayed an endo-mode of action. The N-terminal amino acid sequence data for BGN3.2 and BGN3.4 suggested these two enzymes may be encoded by different genes. The gene encoding the BGN3.2 glucanase was fully sequenced, and its deduced amino acid sequence was similar to those for all other sequenced fungal exo-β-1,3-glucanases. This
BGN3.2 gene consists of an uninterrupted ORF of 2349
bp encoding 783 amino acids possibly with two cleavage sites for the potential removal of a pre- and pro-protein, respectively. A DNA fragment encoding a portion of the
BGN3.4 gene was amplified by PCR, and the nucleotide sequence of this fragment confirmed that BGN3.2 and BGN3.4 are encoded by different genes. The internal peptide sequences of BGN3.3 were not present in the amino acid sequence deduced from the
BGN3.2 gene, reinforcing the view that BGN3.3 is also genetically different to BGN3.2. Genetic differences between multiple forms of fungal β-1,3-glucanases from a single fungus have not been reported previously.</description><identifier>ISSN: 0953-7562</identifier><identifier>EISSN: 1469-8102</identifier><identifier>DOI: 10.1016/j.mycres.2005.08.004</identifier><identifier>PMID: 16431275</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Acremonium ; Acremonium - enzymology ; Acremonium - genetics ; Acremonium - growth & development ; Acremonium blochii ; amino acid sequences ; beta-glucanase ; Fungal glucanases ; fungal proteins ; Glucan 1,3-beta-Glucosidase - chemistry ; Glucan 1,3-beta-Glucosidase - genetics ; Glucan 1,3-beta-Glucosidase - isolation & purification ; Glucan 1,3-beta-Glucosidase - metabolism ; Laminaria digitata ; molecular sequence data ; nucleotide sequences ; sequence analysis ; β-1,3-glucanase genes ; β-1,3-glucanases</subject><ispartof>Mycological research, 2006, Vol.110 (1), p.66-74</ispartof><rights>2005 The British Mycological Society</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-a4460df611681aac92c7bc93252d4b473d0a14884ada427ffa9f5dfe889a26cf3</citedby><cites>FETCH-LOGICAL-c415t-a4460df611681aac92c7bc93252d4b473d0a14884ada427ffa9f5dfe889a26cf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16431275$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Martin, Kirstee L.</creatorcontrib><creatorcontrib>McDougall, Barbara M.</creatorcontrib><creatorcontrib>Unkles, Shiela E.</creatorcontrib><creatorcontrib>Seviour, Robert J.</creatorcontrib><title>The three β-1,3-glucanases from Acremonium blochii strain C59 appear to be encoded by separate genes</title><title>Mycological research</title><addtitle>Mycol Res</addtitle><description>Three exocellular β-1,3-glucanases from
Acremonium blochii strain C59, BGN3.2, BGN3.3 and BGN3.4, were purified. Two, BGN3.2 and BGN3.4 appeared to act as exo-enzymes against laminarin from
Laminaria digitata, while BGN3.3 displayed an endo-mode of action. The N-terminal amino acid sequence data for BGN3.2 and BGN3.4 suggested these two enzymes may be encoded by different genes. The gene encoding the BGN3.2 glucanase was fully sequenced, and its deduced amino acid sequence was similar to those for all other sequenced fungal exo-β-1,3-glucanases. This
BGN3.2 gene consists of an uninterrupted ORF of 2349
bp encoding 783 amino acids possibly with two cleavage sites for the potential removal of a pre- and pro-protein, respectively. A DNA fragment encoding a portion of the
BGN3.4 gene was amplified by PCR, and the nucleotide sequence of this fragment confirmed that BGN3.2 and BGN3.4 are encoded by different genes. The internal peptide sequences of BGN3.3 were not present in the amino acid sequence deduced from the
BGN3.2 gene, reinforcing the view that BGN3.3 is also genetically different to BGN3.2. Genetic differences between multiple forms of fungal β-1,3-glucanases from a single fungus have not been reported previously.</description><subject>Acremonium</subject><subject>Acremonium - enzymology</subject><subject>Acremonium - genetics</subject><subject>Acremonium - growth & development</subject><subject>Acremonium blochii</subject><subject>amino acid sequences</subject><subject>beta-glucanase</subject><subject>Fungal glucanases</subject><subject>fungal proteins</subject><subject>Glucan 1,3-beta-Glucosidase - chemistry</subject><subject>Glucan 1,3-beta-Glucosidase - genetics</subject><subject>Glucan 1,3-beta-Glucosidase - isolation & purification</subject><subject>Glucan 1,3-beta-Glucosidase - metabolism</subject><subject>Laminaria digitata</subject><subject>molecular sequence data</subject><subject>nucleotide sequences</subject><subject>sequence analysis</subject><subject>β-1,3-glucanase genes</subject><subject>β-1,3-glucanases</subject><issn>0953-7562</issn><issn>1469-8102</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqFkUuO1DAQhi0EYpqBGyDwihUJtuMkzgZp1OIljcSCmbVVscvdbiVxsJOR-lochDPhUVpiB6vafPX6P0Jec1ZyxpsPp3I8m4ipFIzVJVMlY_IJ2XHZdIXiTDwlO9bVVdHWjbgiL1I6McYrzqvn5Io3suKirXcE745Il2NEpL9_Ffx9VRyG1cAECRN1MYz0Ji8Zw-TXkfZDMEfvaVoi-Inu647CPCNEugTaI8XJBIuW9meacIYIC9IDTphekmcOhoSvLvWa3H_-dLf_Wtx-__Jtf3NbGMnrpQApG2Zdw3mjOIDphGl701WiFlb2sq0sAy6VkmBBitY56FxtHSrVgWiMq67Ju23uHMPPFdOiR58MDgNMGNakW9ay_Dj7L8jbnJ0SMoNyA00MKUV0eo5-hHjWnOlHD_qkNw_60YNmSmcPue3NZf7aj2j_Nl2Cz8DbDXAQNByiT_r-h8iCGGe1aiuRiY8bgTmwB49RJ-Nzwmh9RLNoG_y_b_gDJESkXA</recordid><startdate>2006</startdate><enddate>2006</enddate><creator>Martin, Kirstee L.</creator><creator>McDougall, Barbara M.</creator><creator>Unkles, Shiela E.</creator><creator>Seviour, Robert J.</creator><general>Elsevier Ltd</general><scope>FBQ</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2006</creationdate><title>The three β-1,3-glucanases from Acremonium blochii strain C59 appear to be encoded by separate genes</title><author>Martin, Kirstee L. ; McDougall, Barbara M. ; Unkles, Shiela E. ; Seviour, Robert J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-a4460df611681aac92c7bc93252d4b473d0a14884ada427ffa9f5dfe889a26cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Acremonium</topic><topic>Acremonium - enzymology</topic><topic>Acremonium - genetics</topic><topic>Acremonium - growth & development</topic><topic>Acremonium blochii</topic><topic>amino acid sequences</topic><topic>beta-glucanase</topic><topic>Fungal glucanases</topic><topic>fungal proteins</topic><topic>Glucan 1,3-beta-Glucosidase - chemistry</topic><topic>Glucan 1,3-beta-Glucosidase - genetics</topic><topic>Glucan 1,3-beta-Glucosidase - isolation & purification</topic><topic>Glucan 1,3-beta-Glucosidase - metabolism</topic><topic>Laminaria digitata</topic><topic>molecular sequence data</topic><topic>nucleotide sequences</topic><topic>sequence analysis</topic><topic>β-1,3-glucanase genes</topic><topic>β-1,3-glucanases</topic><toplevel>online_resources</toplevel><creatorcontrib>Martin, Kirstee L.</creatorcontrib><creatorcontrib>McDougall, Barbara M.</creatorcontrib><creatorcontrib>Unkles, Shiela E.</creatorcontrib><creatorcontrib>Seviour, Robert J.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Mycological research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Martin, Kirstee L.</au><au>McDougall, Barbara M.</au><au>Unkles, Shiela E.</au><au>Seviour, Robert J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The three β-1,3-glucanases from Acremonium blochii strain C59 appear to be encoded by separate genes</atitle><jtitle>Mycological research</jtitle><addtitle>Mycol Res</addtitle><date>2006</date><risdate>2006</risdate><volume>110</volume><issue>1</issue><spage>66</spage><epage>74</epage><pages>66-74</pages><issn>0953-7562</issn><eissn>1469-8102</eissn><abstract>Three exocellular β-1,3-glucanases from
Acremonium blochii strain C59, BGN3.2, BGN3.3 and BGN3.4, were purified. Two, BGN3.2 and BGN3.4 appeared to act as exo-enzymes against laminarin from
Laminaria digitata, while BGN3.3 displayed an endo-mode of action. The N-terminal amino acid sequence data for BGN3.2 and BGN3.4 suggested these two enzymes may be encoded by different genes. The gene encoding the BGN3.2 glucanase was fully sequenced, and its deduced amino acid sequence was similar to those for all other sequenced fungal exo-β-1,3-glucanases. This
BGN3.2 gene consists of an uninterrupted ORF of 2349
bp encoding 783 amino acids possibly with two cleavage sites for the potential removal of a pre- and pro-protein, respectively. A DNA fragment encoding a portion of the
BGN3.4 gene was amplified by PCR, and the nucleotide sequence of this fragment confirmed that BGN3.2 and BGN3.4 are encoded by different genes. The internal peptide sequences of BGN3.3 were not present in the amino acid sequence deduced from the
BGN3.2 gene, reinforcing the view that BGN3.3 is also genetically different to BGN3.2. Genetic differences between multiple forms of fungal β-1,3-glucanases from a single fungus have not been reported previously.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>16431275</pmid><doi>10.1016/j.mycres.2005.08.004</doi><tpages>9</tpages></addata></record> |
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subjects | Acremonium Acremonium - enzymology Acremonium - genetics Acremonium - growth & development Acremonium blochii amino acid sequences beta-glucanase Fungal glucanases fungal proteins Glucan 1,3-beta-Glucosidase - chemistry Glucan 1,3-beta-Glucosidase - genetics Glucan 1,3-beta-Glucosidase - isolation & purification Glucan 1,3-beta-Glucosidase - metabolism Laminaria digitata molecular sequence data nucleotide sequences sequence analysis β-1,3-glucanase genes β-1,3-glucanases |
title | The three β-1,3-glucanases from Acremonium blochii strain C59 appear to be encoded by separate genes |
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