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gene for the heat-shock protein HSP100 is induced by blue light and heat-shock in the fungus Phycomyces blakesleeanus
We cloned and sequenced the Phycomyces hspA gene. The hspA gene product is a 901-amino-acid protein member of the clpB/HSP100 family. HSP100 proteins are ATPases involved in high-temperature tolerance, proteolysis, and protein disaggregation. Phycomyces HSP100 is composed of a domain presumably invo...
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Published in: | Current genetics 2004-11, Vol.46 (5), p.295-303 |
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description | We cloned and sequenced the Phycomyces hspA gene. The hspA gene product is a 901-amino-acid protein member of the clpB/HSP100 family. HSP100 proteins are ATPases involved in high-temperature tolerance, proteolysis, and protein disaggregation. Phycomyces HSP100 is composed of a domain presumably involved in protein-protein interactions and two ATP-binding domains. The hspA promoter contains three heat-shock elements that are presumably involved in the activation of hspA after heat-shock. In addition, four short sequences are present in the hspA promoter and in the promoter of the photoinducible genes carB and carRA; and these are candidates as binding sites for light-regulated transcription factors. Blue light can increase transcription of the hspA gene 10-fold, with a threshold of 1 J/m2. The threshold for hspA photoactivation is 10(4) times higher than the thresholds for blue-light regulation of sporangiophore development and photocarotenogenesis, which suggests that there are differences in the photosensory systems for gene photoactivation and mycelial photoresponses. A heat-shock of 30 min at 34 degrees C or 42 degrees C increased hspA gene activity 160-fold. The differences in maximum hspA gene transcription by blue light and heatshock suggest the presence of different regulatory mechanisms. |
doi_str_mv | 10.1007/s00294-004-0534-4 |
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The hspA gene product is a 901-amino-acid protein member of the clpB/HSP100 family. HSP100 proteins are ATPases involved in high-temperature tolerance, proteolysis, and protein disaggregation. Phycomyces HSP100 is composed of a domain presumably involved in protein-protein interactions and two ATP-binding domains. The hspA promoter contains three heat-shock elements that are presumably involved in the activation of hspA after heat-shock. In addition, four short sequences are present in the hspA promoter and in the promoter of the photoinducible genes carB and carRA; and these are candidates as binding sites for light-regulated transcription factors. Blue light can increase transcription of the hspA gene 10-fold, with a threshold of 1 J/m2. The threshold for hspA photoactivation is 10(4) times higher than the thresholds for blue-light regulation of sporangiophore development and photocarotenogenesis, which suggests that there are differences in the photosensory systems for gene photoactivation and mycelial photoresponses. A heat-shock of 30 min at 34 degrees C or 42 degrees C increased hspA gene activity 160-fold. The differences in maximum hspA gene transcription by blue light and heatshock suggest the presence of different regulatory mechanisms.</description><identifier>ISSN: 0172-8083</identifier><identifier>EISSN: 1432-0983</identifier><identifier>DOI: 10.1007/s00294-004-0534-4</identifier><identifier>PMID: 15526206</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Adenosine Triphosphatases - metabolism ; adenosinetriphosphatase ; Amino Acid Sequence ; amino acid sequences ; Bacterial Proteins ; Base Sequence ; Binding Sites ; blue light ; Carotenoids - biosynthesis ; Carotenoids - radiation effects ; Cloning, Molecular ; gene expression ; Gene Expression Regulation, Fungal - radiation effects ; gene induction ; Genes ; heat shock elements ; heat shock proteins ; heat stress ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - metabolism ; Heat-Shock Response ; High temperature ; Hot Temperature ; hspA gene ; Light ; Molecular Sequence Data ; nucleotide sequences ; Photoactivation ; Photochemistry ; Phycomyces ; Phycomyces - chemistry ; Phycomyces - radiation effects ; Phycomyces blakesleeanus ; promoter regions ; Promoter Regions, Genetic - genetics ; Proteins ; Sequence Homology, Amino Acid ; Transcription, Genetic</subject><ispartof>Current genetics, 2004-11, Vol.46 (5), p.295-303</ispartof><rights>Springer-Verlag 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-f2c46b4d0cac3612bc0f09589b5332cbf7dd5a12e8c59bfb7da5be0c80e1f2c73</citedby><cites>FETCH-LOGICAL-c379t-f2c46b4d0cac3612bc0f09589b5332cbf7dd5a12e8c59bfb7da5be0c80e1f2c73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15526206$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodriguez-Romero, J</creatorcontrib><creatorcontrib>Corrochano, L.M</creatorcontrib><title>gene for the heat-shock protein HSP100 is induced by blue light and heat-shock in the fungus Phycomyces blakesleeanus</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><description>We cloned and sequenced the Phycomyces hspA gene. The hspA gene product is a 901-amino-acid protein member of the clpB/HSP100 family. HSP100 proteins are ATPases involved in high-temperature tolerance, proteolysis, and protein disaggregation. Phycomyces HSP100 is composed of a domain presumably involved in protein-protein interactions and two ATP-binding domains. The hspA promoter contains three heat-shock elements that are presumably involved in the activation of hspA after heat-shock. In addition, four short sequences are present in the hspA promoter and in the promoter of the photoinducible genes carB and carRA; and these are candidates as binding sites for light-regulated transcription factors. Blue light can increase transcription of the hspA gene 10-fold, with a threshold of 1 J/m2. The threshold for hspA photoactivation is 10(4) times higher than the thresholds for blue-light regulation of sporangiophore development and photocarotenogenesis, which suggests that there are differences in the photosensory systems for gene photoactivation and mycelial photoresponses. A heat-shock of 30 min at 34 degrees C or 42 degrees C increased hspA gene activity 160-fold. The differences in maximum hspA gene transcription by blue light and heatshock suggest the presence of different regulatory mechanisms.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>adenosinetriphosphatase</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Bacterial Proteins</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>blue light</subject><subject>Carotenoids - biosynthesis</subject><subject>Carotenoids - radiation effects</subject><subject>Cloning, Molecular</subject><subject>gene expression</subject><subject>Gene Expression Regulation, Fungal - radiation effects</subject><subject>gene induction</subject><subject>Genes</subject><subject>heat shock elements</subject><subject>heat shock proteins</subject><subject>heat stress</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Heat-Shock Response</subject><subject>High temperature</subject><subject>Hot Temperature</subject><subject>hspA gene</subject><subject>Light</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequences</subject><subject>Photoactivation</subject><subject>Photochemistry</subject><subject>Phycomyces</subject><subject>Phycomyces - chemistry</subject><subject>Phycomyces - radiation effects</subject><subject>Phycomyces blakesleeanus</subject><subject>promoter regions</subject><subject>Promoter Regions, Genetic - genetics</subject><subject>Proteins</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transcription, Genetic</subject><issn>0172-8083</issn><issn>1432-0983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQQC0EotvCD-ACFgdugRl_xMkRVYUiVaJS6dmynfEmbTYpcXzYf49XuxIVFw7WXN4ba_QYe4fwGQHMlwQgWlUBlKelqtQLtkElRQVtI1-yDaARVQONPGPnKT0AoGha85qdodaiFlBvWN7SRDzOC1974j25tUr9HB750zKvNEz8-u62_MWHxIepy4E67vfcj5n4OGz7lbupe64V47Ao5mmbE7_t92He7QOlorhHSiORm3J6w15FNyZ6e5oX7P7b1a_L6-rm5_cfl19vqiBNu1ZRBFV71UFwQdYofIAIrW5ar6UUwUfTddqhoCbo1kdvOqc9QWiAsLhGXrBPx73lmt-Z0mp3Qwo0jm6iOSdbG1ErkP8H0WgphGoL-PEf8GHOy1SOsDVKo5XCpkB4hMIyp7RQtE_LsHPL3iLYQzl7LGdLOXsoZ1Vx3p8WZ7-j7q9xSlWAD0cgutm67TIke38nACWU2ig1yj9Ohp0L</recordid><startdate>20041101</startdate><enddate>20041101</enddate><creator>Rodriguez-Romero, J</creator><creator>Corrochano, L.M</creator><general>Springer Nature B.V</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>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>AEUYN</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></search><sort><creationdate>20041101</creationdate><title>gene for the heat-shock protein HSP100 is induced by blue light and heat-shock in the fungus Phycomyces blakesleeanus</title><author>Rodriguez-Romero, J ; Corrochano, L.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-f2c46b4d0cac3612bc0f09589b5332cbf7dd5a12e8c59bfb7da5be0c80e1f2c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>adenosinetriphosphatase</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Bacterial Proteins</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>blue light</topic><topic>Carotenoids - biosynthesis</topic><topic>Carotenoids - radiation effects</topic><topic>Cloning, Molecular</topic><topic>gene expression</topic><topic>Gene Expression Regulation, Fungal - radiation effects</topic><topic>gene induction</topic><topic>Genes</topic><topic>heat shock elements</topic><topic>heat shock proteins</topic><topic>heat stress</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Heat-Shock Response</topic><topic>High temperature</topic><topic>Hot Temperature</topic><topic>hspA gene</topic><topic>Light</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequences</topic><topic>Photoactivation</topic><topic>Photochemistry</topic><topic>Phycomyces</topic><topic>Phycomyces - chemistry</topic><topic>Phycomyces - radiation effects</topic><topic>Phycomyces blakesleeanus</topic><topic>promoter regions</topic><topic>Promoter Regions, Genetic - genetics</topic><topic>Proteins</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodriguez-Romero, J</creatorcontrib><creatorcontrib>Corrochano, L.M</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>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)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</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</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>Biological Sciences</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>Rodriguez-Romero, J</au><au>Corrochano, L.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>gene for the heat-shock protein HSP100 is induced by blue light and heat-shock in the fungus Phycomyces blakesleeanus</atitle><jtitle>Current genetics</jtitle><addtitle>Curr Genet</addtitle><date>2004-11-01</date><risdate>2004</risdate><volume>46</volume><issue>5</issue><spage>295</spage><epage>303</epage><pages>295-303</pages><issn>0172-8083</issn><eissn>1432-0983</eissn><abstract>We cloned and sequenced the Phycomyces hspA gene. The hspA gene product is a 901-amino-acid protein member of the clpB/HSP100 family. HSP100 proteins are ATPases involved in high-temperature tolerance, proteolysis, and protein disaggregation. Phycomyces HSP100 is composed of a domain presumably involved in protein-protein interactions and two ATP-binding domains. The hspA promoter contains three heat-shock elements that are presumably involved in the activation of hspA after heat-shock. In addition, four short sequences are present in the hspA promoter and in the promoter of the photoinducible genes carB and carRA; and these are candidates as binding sites for light-regulated transcription factors. Blue light can increase transcription of the hspA gene 10-fold, with a threshold of 1 J/m2. The threshold for hspA photoactivation is 10(4) times higher than the thresholds for blue-light regulation of sporangiophore development and photocarotenogenesis, which suggests that there are differences in the photosensory systems for gene photoactivation and mycelial photoresponses. A heat-shock of 30 min at 34 degrees C or 42 degrees C increased hspA gene activity 160-fold. The differences in maximum hspA gene transcription by blue light and heatshock suggest the presence of different regulatory mechanisms.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>15526206</pmid><doi>10.1007/s00294-004-0534-4</doi><tpages>9</tpages></addata></record> |
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subjects | Adenosine Triphosphatases - metabolism adenosinetriphosphatase Amino Acid Sequence amino acid sequences Bacterial Proteins Base Sequence Binding Sites blue light Carotenoids - biosynthesis Carotenoids - radiation effects Cloning, Molecular gene expression Gene Expression Regulation, Fungal - radiation effects gene induction Genes heat shock elements heat shock proteins heat stress Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Heat-Shock Response High temperature Hot Temperature hspA gene Light Molecular Sequence Data nucleotide sequences Photoactivation Photochemistry Phycomyces Phycomyces - chemistry Phycomyces - radiation effects Phycomyces blakesleeanus promoter regions Promoter Regions, Genetic - genetics Proteins Sequence Homology, Amino Acid Transcription, Genetic |
title | gene for the heat-shock protein HSP100 is induced by blue light and heat-shock in the fungus Phycomyces blakesleeanus |
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