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
Hauptverfasser: Ishikawa, Kana, Kunitake, Emi, Kawase, Tomomi, Atsumi, Motoki, Noguchi, Yuji, Ishikawa, Shuhei, Ogawa, Masahiro, Koyama, Yasuji, Kimura, Makoto, Kanamaru, Kyoko, Kato, Masashi, Kobayashi, Tetsuo
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container_issue 6
container_start_page 1245
container_title Current genetics
container_volume 64
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.
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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 ; 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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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