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extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription
The gene encoding an acid extracellular protease (AXP) from Yarrowia lipolytica (Candida olea) 148 was cloned and the complete nucleotide sequence was determined. The amino acid sequence deduced from the nucleotide sequence reveals that the mature AXP consists of 353 amino acids with an Mr of 37427....
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| Published in: | Microbiology (Society for General Microbiology) 1996-10, Vol.142 (10), p.2913-2921 |
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| container_end_page | 2921 |
| container_issue | 10 |
| container_start_page | 2913 |
| container_title | Microbiology (Society for General Microbiology) |
| container_volume | 142 |
| creator | Young, T.W Wadeson, A Glover, D.J Quincey, R.V Butlin, M.J Kamei, E.A |
| description | The gene encoding an acid extracellular protease (AXP) from Yarrowia lipolytica (Candida olea) 148 was cloned and the complete nucleotide sequence was determined. The amino acid sequence deduced from the nucleotide sequence reveals that the mature AXP consists of 353 amino acids with an Mr of 37427. The gene also encodes a putative 17 amino acid hydrophobic prepeptide and a 27 amino acid propeptide containing no potential N-glycosylation sites. The mature extracellular enzyme is produced by cleavage between Phe and Ala. AXP is a member of the aspartyl family of proteases. AXP shows homology to proteases of several fungal genera and to human progastricin. The coding sequence is preceded by a potential regulatory region of 1982 bp. Transcription of both AXP and alkaline extracellular protease genes of V. lipolytica 148 is regulated by the pH of culture. |
| doi_str_mv | 10.1099/13500872-142-10-2913 |
| format | article |
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The amino acid sequence deduced from the nucleotide sequence reveals that the mature AXP consists of 353 amino acids with an Mr of 37427. The gene also encodes a putative 17 amino acid hydrophobic prepeptide and a 27 amino acid propeptide containing no potential N-glycosylation sites. The mature extracellular enzyme is produced by cleavage between Phe and Ala. AXP is a member of the aspartyl family of proteases. AXP shows homology to proteases of several fungal genera and to human progastricin. The coding sequence is preceded by a potential regulatory region of 1982 bp. Transcription of both AXP and alkaline extracellular protease genes of V. lipolytica 148 is regulated by the pH of culture.</description><identifier>ISSN: 1350-0872</identifier><identifier>EISSN: 1465-2080</identifier><identifier>DOI: 10.1099/13500872-142-10-2913</identifier><identifier>PMID: 8885407</identifier><language>eng</language><publisher>England: Soc General Microbiol</publisher><subject>Amino Acid Sequence ; Aspartic Acid Endopeptidases - chemistry ; Aspartic Acid Endopeptidases - genetics ; Aspartic Acid Endopeptidases - isolation & purification ; Aspartic Acid Endopeptidases - metabolism ; Base Sequence ; Cloning, Molecular ; Codon ; Fungal Proteins ; genbank/x97068 ; Gene Expression Regulation, Fungal ; Genes, Fungal - genetics ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Molecular Weight ; plant biochemistry ; plant breeding ; plant genetics ; plant physiology ; Protein Precursors - genetics ; Protein Processing, Post-Translational ; RNA, Fungal - analysis ; RNA, Messenger - analysis ; Saccharomycetales - enzymology ; Saccharomycetales - genetics ; Sequence Alignment ; Sequence Analysis ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Transcription, Genetic ; Yeasts - enzymology ; Yeasts - genetics</subject><ispartof>Microbiology (Society for General Microbiology), 1996-10, Vol.142 (10), p.2913-2921</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c407t-e6fdaf91b53a01b88514c4a49e1a99f6c533cd9ce076349d46006198eb369ab53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8885407$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Young, T.W</creatorcontrib><creatorcontrib>Wadeson, A</creatorcontrib><creatorcontrib>Glover, D.J</creatorcontrib><creatorcontrib>Quincey, R.V</creatorcontrib><creatorcontrib>Butlin, M.J</creatorcontrib><creatorcontrib>Kamei, E.A</creatorcontrib><title>extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription</title><title>Microbiology (Society for General Microbiology)</title><addtitle>Microbiology</addtitle><description>The gene encoding an acid extracellular protease (AXP) from Yarrowia lipolytica (Candida olea) 148 was cloned and the complete nucleotide sequence was determined. The amino acid sequence deduced from the nucleotide sequence reveals that the mature AXP consists of 353 amino acids with an Mr of 37427. The gene also encodes a putative 17 amino acid hydrophobic prepeptide and a 27 amino acid propeptide containing no potential N-glycosylation sites. The mature extracellular enzyme is produced by cleavage between Phe and Ala. AXP is a member of the aspartyl family of proteases. AXP shows homology to proteases of several fungal genera and to human progastricin. The coding sequence is preceded by a potential regulatory region of 1982 bp. Transcription of both AXP and alkaline extracellular protease genes of V. lipolytica 148 is regulated by the pH of culture.</description><subject>Amino Acid Sequence</subject><subject>Aspartic Acid Endopeptidases - chemistry</subject><subject>Aspartic Acid Endopeptidases - genetics</subject><subject>Aspartic Acid Endopeptidases - isolation & purification</subject><subject>Aspartic Acid Endopeptidases - metabolism</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>Codon</subject><subject>Fungal Proteins</subject><subject>genbank/x97068</subject><subject>Gene Expression Regulation, Fungal</subject><subject>Genes, Fungal - genetics</subject><subject>Hydrogen-Ion Concentration</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>plant biochemistry</subject><subject>plant breeding</subject><subject>plant genetics</subject><subject>plant physiology</subject><subject>Protein Precursors - genetics</subject><subject>Protein Processing, Post-Translational</subject><subject>RNA, Fungal - analysis</subject><subject>RNA, Messenger - analysis</subject><subject>Saccharomycetales - enzymology</subject><subject>Saccharomycetales - genetics</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transcription, Genetic</subject><subject>Yeasts - enzymology</subject><subject>Yeasts - genetics</subject><issn>1350-0872</issn><issn>1465-2080</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNpVUE1P3DAQtVARpZR_QIVPPVQKjGPnw71VqC2VkDhQDj2ZiTNZjLLx1s4K-PedaLeVerBs-X3MmyfEmYILBdZeKl0BtE1ZKMMHitIqfSCOlamrooQW3vCbKcXCeSve5fwEwCCoI3HUtm1loDkWD_QyJ_Q0jtsRk0QferlJcSbMJFc0kYyD_IUpxeeAcgybOL7OweNnmen3liZPEieWXBeJVmwxUy_ZcMo-hc0c4vReHA44Zjrd3yfi_tvXn1fXxc3t9x9XX24Kzznmguqhx8GqrtIIquN4yniDxpJCa4faV1r73nqCptbG9rwH1Mq21OnaIqtOxMedL6fnYHl265CXvXCiuM2uaU1Tm1Iz0eyIPsWcEw1uk8Ia06tT4JZi3d9iHRe7fC7FsuzD3n_bran_J9o3yfinHf4YVo_PIZHj9taBh3Qhchb_v9n5jjxgdLhKIbv7uxKUhrLlkE2j_wBnQowp</recordid><startdate>19961001</startdate><enddate>19961001</enddate><creator>Young, T.W</creator><creator>Wadeson, A</creator><creator>Glover, D.J</creator><creator>Quincey, R.V</creator><creator>Butlin, M.J</creator><creator>Kamei, E.A</creator><general>Soc General Microbiol</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>7X8</scope></search><sort><creationdate>19961001</creationdate><title>extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription</title><author>Young, T.W ; Wadeson, A ; Glover, D.J ; Quincey, R.V ; Butlin, M.J ; Kamei, E.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c407t-e6fdaf91b53a01b88514c4a49e1a99f6c533cd9ce076349d46006198eb369ab53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Aspartic Acid Endopeptidases - chemistry</topic><topic>Aspartic Acid Endopeptidases - genetics</topic><topic>Aspartic Acid Endopeptidases - isolation & purification</topic><topic>Aspartic Acid Endopeptidases - metabolism</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>Codon</topic><topic>Fungal Proteins</topic><topic>genbank/x97068</topic><topic>Gene Expression Regulation, Fungal</topic><topic>Genes, Fungal - genetics</topic><topic>Hydrogen-Ion Concentration</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>plant biochemistry</topic><topic>plant breeding</topic><topic>plant genetics</topic><topic>plant physiology</topic><topic>Protein Precursors - genetics</topic><topic>Protein Processing, Post-Translational</topic><topic>RNA, Fungal - analysis</topic><topic>RNA, Messenger - analysis</topic><topic>Saccharomycetales - enzymology</topic><topic>Saccharomycetales - genetics</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transcription, Genetic</topic><topic>Yeasts - enzymology</topic><topic>Yeasts - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Young, T.W</creatorcontrib><creatorcontrib>Wadeson, A</creatorcontrib><creatorcontrib>Glover, D.J</creatorcontrib><creatorcontrib>Quincey, R.V</creatorcontrib><creatorcontrib>Butlin, M.J</creatorcontrib><creatorcontrib>Kamei, E.A</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>MEDLINE - Academic</collection><jtitle>Microbiology (Society for General Microbiology)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Young, T.W</au><au>Wadeson, A</au><au>Glover, D.J</au><au>Quincey, R.V</au><au>Butlin, M.J</au><au>Kamei, E.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription</atitle><jtitle>Microbiology (Society for General Microbiology)</jtitle><addtitle>Microbiology</addtitle><date>1996-10-01</date><risdate>1996</risdate><volume>142</volume><issue>10</issue><spage>2913</spage><epage>2921</epage><pages>2913-2921</pages><issn>1350-0872</issn><eissn>1465-2080</eissn><abstract>The gene encoding an acid extracellular protease (AXP) from Yarrowia lipolytica (Candida olea) 148 was cloned and the complete nucleotide sequence was determined. The amino acid sequence deduced from the nucleotide sequence reveals that the mature AXP consists of 353 amino acids with an Mr of 37427. The gene also encodes a putative 17 amino acid hydrophobic prepeptide and a 27 amino acid propeptide containing no potential N-glycosylation sites. The mature extracellular enzyme is produced by cleavage between Phe and Ala. AXP is a member of the aspartyl family of proteases. AXP shows homology to proteases of several fungal genera and to human progastricin. The coding sequence is preceded by a potential regulatory region of 1982 bp. Transcription of both AXP and alkaline extracellular protease genes of V. lipolytica 148 is regulated by the pH of culture.</abstract><cop>England</cop><pub>Soc General Microbiol</pub><pmid>8885407</pmid><doi>10.1099/13500872-142-10-2913</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1350-0872 |
| ispartof | Microbiology (Society for General Microbiology), 1996-10, Vol.142 (10), p.2913-2921 |
| issn | 1350-0872 1465-2080 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78476423 |
| source | Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Aspartic Acid Endopeptidases - chemistry Aspartic Acid Endopeptidases - genetics Aspartic Acid Endopeptidases - isolation & purification Aspartic Acid Endopeptidases - metabolism Base Sequence Cloning, Molecular Codon Fungal Proteins genbank/x97068 Gene Expression Regulation, Fungal Genes, Fungal - genetics Hydrogen-Ion Concentration Molecular Sequence Data Molecular Weight plant biochemistry plant breeding plant genetics plant physiology Protein Precursors - genetics Protein Processing, Post-Translational RNA, Fungal - analysis RNA, Messenger - analysis Saccharomycetales - enzymology Saccharomycetales - genetics Sequence Alignment Sequence Analysis Sequence Analysis, DNA Sequence Homology, Amino Acid Transcription, Genetic Yeasts - enzymology Yeasts - genetics |
| title | extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription |
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