Molecular cloning of the gene encoding an outer-membrane-associated beta-N-acetylglucosaminidase involved in chitin degradation system of Alteromonas sp. strain O-7
The gene encoding β-N-acetylglucosaminidase (GlcNAcaseA) was cloned using PCR with degenerate oligonucleotide primers from the partial amino acid sequence of the enzyme. The gene encoded a polypeptide of 863 amino acids with a predicted molecular mass of 97 kDa. A characteristic signal peptide, whic...
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Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2000, Vol.64 (11), p.2512-2516 |
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creator | Tsujibo, H. (Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan)) Miyamoto, J Kondo, N Miyamoto, K Baba, N Inamori, Y |
description | The gene encoding β-N-acetylglucosaminidase (GlcNAcaseA) was cloned using PCR with degenerate oligonucleotide primers from the partial amino acid sequence of the enzyme. The gene encoded a polypeptide of 863 amino acids with a predicted molecular mass of 97 kDa. A characteristic signal peptide, which was present at the amino-terminus of the precursor protein, contained four amino acids (Ala-Gly-Cys-Ser) identical in sequence and location to the processing and modification sites of the outer membrane lipoprotein of Escherichia coli, indicating that the mature GlcNAcaseA is a lipoprotein the N-terminal cysteine residue of which would be modified by the fatty acid that anchors the protein in the membrane. The predicted amino acid sequence of GlcNAcaseA showed similarity to bacterial β-N-acetylglucosaminidases belonging to the family 20 glycosyl hydrolases. |
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(Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan)) ; Miyamoto, J ; Kondo, N ; Miyamoto, K ; Baba, N ; Inamori, Y</creator><creatorcontrib>Tsujibo, H. (Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan)) ; Miyamoto, J ; Kondo, N ; Miyamoto, K ; Baba, N ; Inamori, Y</creatorcontrib><description>The gene encoding β-N-acetylglucosaminidase (GlcNAcaseA) was cloned using PCR with degenerate oligonucleotide primers from the partial amino acid sequence of the enzyme. The gene encoded a polypeptide of 863 amino acids with a predicted molecular mass of 97 kDa. A characteristic signal peptide, which was present at the amino-terminus of the precursor protein, contained four amino acids (Ala-Gly-Cys-Ser) identical in sequence and location to the processing and modification sites of the outer membrane lipoprotein of Escherichia coli, indicating that the mature GlcNAcaseA is a lipoprotein the N-terminal cysteine residue of which would be modified by the fatty acid that anchors the protein in the membrane. The predicted amino acid sequence of GlcNAcaseA showed similarity to bacterial β-N-acetylglucosaminidases belonging to the family 20 glycosyl hydrolases.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.64.2512</identifier><identifier>PMID: 11193430</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Acetylglucosaminidase - genetics ; Acetylglucosaminidase - metabolism ; Alteromonas ; Alteromonas - enzymology ; Alteromonas - genetics ; Alteromonas sp. O-7 ; Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; CHITIN ; Chitin - metabolism ; chitin degradation ; Cloning, Molecular ; DEGRADATION ; Fundamental and applied biological sciences. Psychology ; Genetics ; GRAM NEGATIVE BACTERIA ; lipoprotein ; LIPOPROTEINS ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mission oriented research ; MOLECULAR CLONING ; Molecular Sequence Data ; Restriction Mapping ; Sequence Homology, Amino Acid ; β-N-acetylglucosaminidase</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2000, Vol.64 (11), p.2512-2516</ispartof><rights>2000 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2000</rights><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c617t-221e7caf2e348dda8b35091610c8213c5db9eb4dd731929cbb6c5ea1101b452d3</citedby><cites>FETCH-LOGICAL-c617t-221e7caf2e348dda8b35091610c8213c5db9eb4dd731929cbb6c5ea1101b452d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=910800$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11193430$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsujibo, H. (Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan))</creatorcontrib><creatorcontrib>Miyamoto, J</creatorcontrib><creatorcontrib>Kondo, N</creatorcontrib><creatorcontrib>Miyamoto, K</creatorcontrib><creatorcontrib>Baba, N</creatorcontrib><creatorcontrib>Inamori, Y</creatorcontrib><title>Molecular cloning of the gene encoding an outer-membrane-associated beta-N-acetylglucosaminidase involved in chitin degradation system of Alteromonas sp. strain O-7</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>The gene encoding β-N-acetylglucosaminidase (GlcNAcaseA) was cloned using PCR with degenerate oligonucleotide primers from the partial amino acid sequence of the enzyme. The gene encoded a polypeptide of 863 amino acids with a predicted molecular mass of 97 kDa. A characteristic signal peptide, which was present at the amino-terminus of the precursor protein, contained four amino acids (Ala-Gly-Cys-Ser) identical in sequence and location to the processing and modification sites of the outer membrane lipoprotein of Escherichia coli, indicating that the mature GlcNAcaseA is a lipoprotein the N-terminal cysteine residue of which would be modified by the fatty acid that anchors the protein in the membrane. The predicted amino acid sequence of GlcNAcaseA showed similarity to bacterial β-N-acetylglucosaminidases belonging to the family 20 glycosyl hydrolases.</description><subject>Acetylglucosaminidase - genetics</subject><subject>Acetylglucosaminidase - metabolism</subject><subject>Alteromonas</subject><subject>Alteromonas - enzymology</subject><subject>Alteromonas - genetics</subject><subject>Alteromonas sp. O-7</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>CHITIN</subject><subject>Chitin - metabolism</subject><subject>chitin degradation</subject><subject>Cloning, Molecular</subject><subject>DEGRADATION</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics</subject><subject>GRAM NEGATIVE BACTERIA</subject><subject>lipoprotein</subject><subject>LIPOPROTEINS</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mission oriented research</subject><subject>MOLECULAR CLONING</subject><subject>Molecular Sequence Data</subject><subject>Restriction Mapping</subject><subject>Sequence Homology, Amino Acid</subject><subject>β-N-acetylglucosaminidase</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U2LFDEQBuBGFHdcPXlWAgtepMd8dHe6j8viJ6vrQc9NJamejaSTMUmvzP_xh5pmRr0IngqKp6pI3qp6yuiWccleKaW2XbPlLeP3qg0Tjay7oZH3qw0dWFf3TcvOqkcpfaO0NFr2sDpjjA2iEXRT_fwYHOrFQSTaBW_9joSJ5FskO_RI0Otg1iZ4EpaMsZ5xVhE81pBS0BYyGqIwQ_2pBo354HZu0SHBbL01kJBYfxfcXVHWE31rcykGdxEMZBs8SYeUcV6PXrqyP8zBQyJpvyUpRyj4ppaPqwcTuIRPTvW8-vrm9Zerd_X1zdv3V5fXte6YzDXnDKWGiaNoemOgV6Jdv4BR3XMmdGvUgKoxRgo28EEr1ekWgTHKVNNyI86rF8e9-xi-L5jyONuk0bny3rCkUfKWCzk0_4VM9lwKLgp8eYQ6hpQiTuM-2hniYWR0XNMbS3pj14xrekU_P61d1Izmrz3FVcDFCUDS4KYShLbpjxsY7emquqOyfgpxhh8hOjNmOLgQf4-If99_dhycIIywi8V9-MwpZZRy2Q3iF025wAY</recordid><startdate>2000</startdate><enddate>2000</enddate><creator>Tsujibo, H. (Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan))</creator><creator>Miyamoto, J</creator><creator>Kondo, N</creator><creator>Miyamoto, K</creator><creator>Baba, N</creator><creator>Inamori, Y</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><scope>FBQ</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>C1K</scope><scope>7X8</scope></search><sort><creationdate>2000</creationdate><title>Molecular cloning of the gene encoding an outer-membrane-associated beta-N-acetylglucosaminidase involved in chitin degradation system of Alteromonas sp. strain O-7</title><author>Tsujibo, H. (Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan)) ; Miyamoto, J ; Kondo, N ; Miyamoto, K ; Baba, N ; Inamori, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c617t-221e7caf2e348dda8b35091610c8213c5db9eb4dd731929cbb6c5ea1101b452d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Acetylglucosaminidase - genetics</topic><topic>Acetylglucosaminidase - metabolism</topic><topic>Alteromonas</topic><topic>Alteromonas - enzymology</topic><topic>Alteromonas - genetics</topic><topic>Alteromonas sp. O-7</topic><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>CHITIN</topic><topic>Chitin - metabolism</topic><topic>chitin degradation</topic><topic>Cloning, Molecular</topic><topic>DEGRADATION</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetics</topic><topic>GRAM NEGATIVE BACTERIA</topic><topic>lipoprotein</topic><topic>LIPOPROTEINS</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mission oriented research</topic><topic>MOLECULAR CLONING</topic><topic>Molecular Sequence Data</topic><topic>Restriction Mapping</topic><topic>Sequence Homology, Amino Acid</topic><topic>β-N-acetylglucosaminidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsujibo, H. (Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan))</creatorcontrib><creatorcontrib>Miyamoto, J</creatorcontrib><creatorcontrib>Kondo, N</creatorcontrib><creatorcontrib>Miyamoto, K</creatorcontrib><creatorcontrib>Baba, N</creatorcontrib><creatorcontrib>Inamori, Y</creatorcontrib><collection>AGRIS</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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tsujibo, H. (Osaka Univ. of Pharmaceutical Sciences, Takatsuki (Japan))</au><au>Miyamoto, J</au><au>Kondo, N</au><au>Miyamoto, K</au><au>Baba, N</au><au>Inamori, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning of the gene encoding an outer-membrane-associated beta-N-acetylglucosaminidase involved in chitin degradation system of Alteromonas sp. strain O-7</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2000</date><risdate>2000</risdate><volume>64</volume><issue>11</issue><spage>2512</spage><epage>2516</epage><pages>2512-2516</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>The gene encoding β-N-acetylglucosaminidase (GlcNAcaseA) was cloned using PCR with degenerate oligonucleotide primers from the partial amino acid sequence of the enzyme. The gene encoded a polypeptide of 863 amino acids with a predicted molecular mass of 97 kDa. A characteristic signal peptide, which was present at the amino-terminus of the precursor protein, contained four amino acids (Ala-Gly-Cys-Ser) identical in sequence and location to the processing and modification sites of the outer membrane lipoprotein of Escherichia coli, indicating that the mature GlcNAcaseA is a lipoprotein the N-terminal cysteine residue of which would be modified by the fatty acid that anchors the protein in the membrane. The predicted amino acid sequence of GlcNAcaseA showed similarity to bacterial β-N-acetylglucosaminidases belonging to the family 20 glycosyl hydrolases.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>11193430</pmid><doi>10.1271/bbb.64.2512</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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source | Freely Accessible Japanese Titles (ERDB Project); MEDLINE; Full-Text Journals in Chemistry (Open access); J-STAGE日本語サイト (Free Access); EZB Electronic Journals Library; Oxford Journals |
subjects | Acetylglucosaminidase - genetics Acetylglucosaminidase - metabolism Alteromonas Alteromonas - enzymology Alteromonas - genetics Alteromonas sp. O-7 Amino Acid Sequence Base Sequence Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology CHITIN Chitin - metabolism chitin degradation Cloning, Molecular DEGRADATION Fundamental and applied biological sciences. Psychology Genetics GRAM NEGATIVE BACTERIA lipoprotein LIPOPROTEINS Membrane Proteins - genetics Membrane Proteins - metabolism Mission oriented research MOLECULAR CLONING Molecular Sequence Data Restriction Mapping Sequence Homology, Amino Acid β-N-acetylglucosaminidase |
title | Molecular cloning of the gene encoding an outer-membrane-associated beta-N-acetylglucosaminidase involved in chitin degradation system of Alteromonas sp. strain O-7 |
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