Comparison of the paralogous transcription factors AraR and XlnR in Aspergillus oryzae
The paralogous transcription factors AraR and XlnR in Aspergillus regulate genes that are involved in degradation of cellulose and hemicellulose and catabolism of pentose. AraR and XlnR target the same genes for pentose catabolism but target different genes encoding enzymes for polysaccharide degrad...
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Veröffentlicht in: | Current genetics 2018-12, Vol.64 (6), p.1245-1260 |
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creator | Ishikawa, Kana Kunitake, Emi Kawase, Tomomi Atsumi, Motoki Noguchi, Yuji Ishikawa, Shuhei Ogawa, Masahiro Koyama, Yasuji Kimura, Makoto Kanamaru, Kyoko Kato, Masashi Kobayashi, Tetsuo |
description | The paralogous transcription factors AraR and XlnR in
Aspergillus
regulate genes that are involved in degradation of cellulose and hemicellulose and catabolism of pentose. AraR and XlnR target the same genes for pentose catabolism but target different genes encoding enzymes for polysaccharide degradation. To uncover the relationship between these paralogous transcription factors, we examined their contribution to regulation of the PCP genes and compared their preferred recognition sequences. Both AraR and XlnR are involved in induction of all the pentose catabolic genes in
A. oryzae
except
larA
encoding
l
-arabinose reductase, which was regulated by AraR but not by XlnR. DNA-binding studies revealed that the recognition sequences of AraR and XlnR also differ only slightly; AraR prefers CGGDTAAW, while XlnR prefers CGGNTAAW. All the pentose catabolic genes possess at least one recognition site to which both AraR and XlnR can bind. Cooperative binding by the factors was not observed. Instead, they competed to bind to the shared sites. XlnR bound to the recognition sites mentioned above as a monomer, but bound to the sequence TTAGSCTAA on the xylanase promoters as a dimer. Consequently, AraR and XlnR have significantly similar, but not the same, DNA-binding properties. Such a slight difference in these paralogous transcription factors may lead to complex outputs in enzyme production depending on the concentrations of coexisting inducer molecules in the natural environment. |
doi_str_mv | 10.1007/s00294-018-0837-5 |
format | Article |
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Aspergillus
regulate genes that are involved in degradation of cellulose and hemicellulose and catabolism of pentose. AraR and XlnR target the same genes for pentose catabolism but target different genes encoding enzymes for polysaccharide degradation. To uncover the relationship between these paralogous transcription factors, we examined their contribution to regulation of the PCP genes and compared their preferred recognition sequences. Both AraR and XlnR are involved in induction of all the pentose catabolic genes in
A. oryzae
except
larA
encoding
l
-arabinose reductase, which was regulated by AraR but not by XlnR. DNA-binding studies revealed that the recognition sequences of AraR and XlnR also differ only slightly; AraR prefers CGGDTAAW, while XlnR prefers CGGNTAAW. All the pentose catabolic genes possess at least one recognition site to which both AraR and XlnR can bind. Cooperative binding by the factors was not observed. Instead, they competed to bind to the shared sites. XlnR bound to the recognition sites mentioned above as a monomer, but bound to the sequence TTAGSCTAA on the xylanase promoters as a dimer. Consequently, AraR and XlnR have significantly similar, but not the same, DNA-binding properties. Such a slight difference in these paralogous transcription factors may lead to complex outputs in enzyme production depending on the concentrations of coexisting inducer molecules in the natural environment.</description><identifier>ISSN: 0172-8083</identifier><identifier>EISSN: 1432-0983</identifier><identifier>DOI: 10.1007/s00294-018-0837-5</identifier><identifier>PMID: 29654355</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Arabinose ; Aspergillus oryzae - chemistry ; Aspergillus oryzae - genetics ; Aspergillus oryzae - metabolism ; Binding ; Biochemistry ; Biomedical and Life Sciences ; Catabolism ; Cell Biology ; Cellulose ; Degradation ; Deoxyribonucleic acid ; DNA ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Gene expression ; Gene Expression Regulation, Fungal - physiology ; Gene regulation ; Gene sequencing ; Genes ; Hemicellulose ; Life Sciences ; Microbial Genetics and Genomics ; Microbiology ; Natural environment ; Nucleotide sequence ; Original Article ; Pentose ; Pentose Phosphate Pathway - physiology ; Plant Sciences ; Protein Multimerization - physiology ; Proteomics ; Recognition ; Reductase ; Response Elements ; Trans-Activators - chemistry ; Trans-Activators - genetics ; Trans-Activators - metabolism ; Transcription factors ; Xylanase</subject><ispartof>Current genetics, 2018-12, Vol.64 (6), p.1245-1260</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018</rights><rights>Current Genetics is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-936e78587279114eed28eab2824e8a9a65361f01c033591ef59f7c4601ae2d2a3</citedby><cites>FETCH-LOGICAL-c482t-936e78587279114eed28eab2824e8a9a65361f01c033591ef59f7c4601ae2d2a3</cites><orcidid>0000-0002-4008-454X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00294-018-0837-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00294-018-0837-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27929,27930,41493,42562,51324</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29654355$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ishikawa, Kana</creatorcontrib><creatorcontrib>Kunitake, Emi</creatorcontrib><creatorcontrib>Kawase, Tomomi</creatorcontrib><creatorcontrib>Atsumi, Motoki</creatorcontrib><creatorcontrib>Noguchi, Yuji</creatorcontrib><creatorcontrib>Ishikawa, Shuhei</creatorcontrib><creatorcontrib>Ogawa, Masahiro</creatorcontrib><creatorcontrib>Koyama, Yasuji</creatorcontrib><creatorcontrib>Kimura, Makoto</creatorcontrib><creatorcontrib>Kanamaru, Kyoko</creatorcontrib><creatorcontrib>Kato, Masashi</creatorcontrib><creatorcontrib>Kobayashi, Tetsuo</creatorcontrib><title>Comparison of the paralogous transcription factors AraR and XlnR in Aspergillus oryzae</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><addtitle>Curr Genet</addtitle><description>The paralogous transcription factors AraR and XlnR in
Aspergillus
regulate genes that are involved in degradation of cellulose and hemicellulose and catabolism of pentose. AraR and XlnR target the same genes for pentose catabolism but target different genes encoding enzymes for polysaccharide degradation. To uncover the relationship between these paralogous transcription factors, we examined their contribution to regulation of the PCP genes and compared their preferred recognition sequences. Both AraR and XlnR are involved in induction of all the pentose catabolic genes in
A. oryzae
except
larA
encoding
l
-arabinose reductase, which was regulated by AraR but not by XlnR. DNA-binding studies revealed that the recognition sequences of AraR and XlnR also differ only slightly; AraR prefers CGGDTAAW, while XlnR prefers CGGNTAAW. All the pentose catabolic genes possess at least one recognition site to which both AraR and XlnR can bind. Cooperative binding by the factors was not observed. Instead, they competed to bind to the shared sites. XlnR bound to the recognition sites mentioned above as a monomer, but bound to the sequence TTAGSCTAA on the xylanase promoters as a dimer. Consequently, AraR and XlnR have significantly similar, but not the same, DNA-binding properties. Such a slight difference in these paralogous transcription factors may lead to complex outputs in enzyme production depending on the concentrations of coexisting inducer molecules in the natural environment.</description><subject>Arabinose</subject><subject>Aspergillus oryzae - chemistry</subject><subject>Aspergillus oryzae - genetics</subject><subject>Aspergillus oryzae - metabolism</subject><subject>Binding</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Catabolism</subject><subject>Cell Biology</subject><subject>Cellulose</subject><subject>Degradation</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Fungal - physiology</subject><subject>Gene regulation</subject><subject>Gene sequencing</subject><subject>Genes</subject><subject>Hemicellulose</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Natural environment</subject><subject>Nucleotide sequence</subject><subject>Original Article</subject><subject>Pentose</subject><subject>Pentose Phosphate Pathway - physiology</subject><subject>Plant Sciences</subject><subject>Protein Multimerization - physiology</subject><subject>Proteomics</subject><subject>Recognition</subject><subject>Reductase</subject><subject>Response Elements</subject><subject>Trans-Activators - chemistry</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription factors</subject><subject>Xylanase</subject><issn>0172-8083</issn><issn>1432-0983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kEtLAzEUhYMotj5-gBsJuHEzevOaJMtSfEFBEBV3IU7v1JHpZEymC_31ptQHCK4u4Xzn3JtDyBGDMwagzxMAt7IAZgowQhdqi4yZFLwAa8Q2GQPTvDBZGpG9lF4BGDdW75IRt6WSQqkxeZyGZe9jk0JHQ02HF6T56duwCKtEh-i7VMWmH5qs174aQkx0Ev0d9d2cPrXdHW06Okk9xkXTttkS4vuHxwOyU_s24eHX3CcPlxf30-tidnt1M53MikoaPhRWlKiNMppry5hEnHOD_pkbLtF460slSlYDq0AIZRnWyta6kiUwj3zOvdgnp5vcPoa3FabBLZtUYdv6DvMHHAeuBLMKdEZP_qCvYRW7fN2akmUphGSZYhuqiiGliLXrY7P08d0xcOvS3aZ0l0t369Kdyp7jr-TV8xLnP47vljPAN0DKUrfA-Lv6_9RPHPGLWg</recordid><startdate>20181201</startdate><enddate>20181201</enddate><creator>Ishikawa, Kana</creator><creator>Kunitake, Emi</creator><creator>Kawase, Tomomi</creator><creator>Atsumi, Motoki</creator><creator>Noguchi, Yuji</creator><creator>Ishikawa, Shuhei</creator><creator>Ogawa, Masahiro</creator><creator>Koyama, Yasuji</creator><creator>Kimura, Makoto</creator><creator>Kanamaru, Kyoko</creator><creator>Kato, Masashi</creator><creator>Kobayashi, Tetsuo</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><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>3V.</scope><scope>7QL</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4008-454X</orcidid></search><sort><creationdate>20181201</creationdate><title>Comparison of the paralogous transcription factors AraR and XlnR in Aspergillus oryzae</title><author>Ishikawa, Kana ; Kunitake, Emi ; Kawase, Tomomi ; Atsumi, Motoki ; Noguchi, Yuji ; Ishikawa, Shuhei ; Ogawa, Masahiro ; Koyama, Yasuji ; Kimura, Makoto ; Kanamaru, Kyoko ; Kato, Masashi ; Kobayashi, Tetsuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-936e78587279114eed28eab2824e8a9a65361f01c033591ef59f7c4601ae2d2a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Arabinose</topic><topic>Aspergillus oryzae - chemistry</topic><topic>Aspergillus oryzae - genetics</topic><topic>Aspergillus oryzae - metabolism</topic><topic>Binding</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Catabolism</topic><topic>Cell Biology</topic><topic>Cellulose</topic><topic>Degradation</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Fungal - physiology</topic><topic>Gene regulation</topic><topic>Gene sequencing</topic><topic>Genes</topic><topic>Hemicellulose</topic><topic>Life Sciences</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Natural environment</topic><topic>Nucleotide sequence</topic><topic>Original Article</topic><topic>Pentose</topic><topic>Pentose Phosphate Pathway - physiology</topic><topic>Plant Sciences</topic><topic>Protein Multimerization - physiology</topic><topic>Proteomics</topic><topic>Recognition</topic><topic>Reductase</topic><topic>Response Elements</topic><topic>Trans-Activators - chemistry</topic><topic>Trans-Activators - genetics</topic><topic>Trans-Activators - metabolism</topic><topic>Transcription factors</topic><topic>Xylanase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ishikawa, Kana</creatorcontrib><creatorcontrib>Kunitake, Emi</creatorcontrib><creatorcontrib>Kawase, Tomomi</creatorcontrib><creatorcontrib>Atsumi, Motoki</creatorcontrib><creatorcontrib>Noguchi, Yuji</creatorcontrib><creatorcontrib>Ishikawa, Shuhei</creatorcontrib><creatorcontrib>Ogawa, Masahiro</creatorcontrib><creatorcontrib>Koyama, Yasuji</creatorcontrib><creatorcontrib>Kimura, Makoto</creatorcontrib><creatorcontrib>Kanamaru, Kyoko</creatorcontrib><creatorcontrib>Kato, Masashi</creatorcontrib><creatorcontrib>Kobayashi, Tetsuo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>Proquest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Current genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ishikawa, Kana</au><au>Kunitake, Emi</au><au>Kawase, Tomomi</au><au>Atsumi, Motoki</au><au>Noguchi, Yuji</au><au>Ishikawa, Shuhei</au><au>Ogawa, Masahiro</au><au>Koyama, Yasuji</au><au>Kimura, Makoto</au><au>Kanamaru, Kyoko</au><au>Kato, Masashi</au><au>Kobayashi, Tetsuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparison of the paralogous transcription factors AraR and XlnR in Aspergillus oryzae</atitle><jtitle>Current genetics</jtitle><stitle>Curr Genet</stitle><addtitle>Curr Genet</addtitle><date>2018-12-01</date><risdate>2018</risdate><volume>64</volume><issue>6</issue><spage>1245</spage><epage>1260</epage><pages>1245-1260</pages><issn>0172-8083</issn><eissn>1432-0983</eissn><abstract>The paralogous transcription factors AraR and XlnR in
Aspergillus
regulate genes that are involved in degradation of cellulose and hemicellulose and catabolism of pentose. AraR and XlnR target the same genes for pentose catabolism but target different genes encoding enzymes for polysaccharide degradation. To uncover the relationship between these paralogous transcription factors, we examined their contribution to regulation of the PCP genes and compared their preferred recognition sequences. Both AraR and XlnR are involved in induction of all the pentose catabolic genes in
A. oryzae
except
larA
encoding
l
-arabinose reductase, which was regulated by AraR but not by XlnR. DNA-binding studies revealed that the recognition sequences of AraR and XlnR also differ only slightly; AraR prefers CGGDTAAW, while XlnR prefers CGGNTAAW. All the pentose catabolic genes possess at least one recognition site to which both AraR and XlnR can bind. Cooperative binding by the factors was not observed. Instead, they competed to bind to the shared sites. XlnR bound to the recognition sites mentioned above as a monomer, but bound to the sequence TTAGSCTAA on the xylanase promoters as a dimer. Consequently, AraR and XlnR have significantly similar, but not the same, DNA-binding properties. Such a slight difference in these paralogous transcription factors may lead to complex outputs in enzyme production depending on the concentrations of coexisting inducer molecules in the natural environment.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29654355</pmid><doi>10.1007/s00294-018-0837-5</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0002-4008-454X</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Arabinose Aspergillus oryzae - chemistry Aspergillus oryzae - genetics Aspergillus oryzae - metabolism Binding Biochemistry Biomedical and Life Sciences Catabolism Cell Biology Cellulose Degradation Deoxyribonucleic acid DNA Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Gene expression Gene Expression Regulation, Fungal - physiology Gene regulation Gene sequencing Genes Hemicellulose Life Sciences Microbial Genetics and Genomics Microbiology Natural environment Nucleotide sequence Original Article Pentose Pentose Phosphate Pathway - physiology Plant Sciences Protein Multimerization - physiology Proteomics Recognition Reductase Response Elements Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - metabolism Transcription factors Xylanase |
title | Comparison of the paralogous transcription factors AraR and XlnR in Aspergillus oryzae |
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