A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock
The heat-shock response is characterized by the expression of a set of classical heat-shock genes, and is regulated by heat-shock transcription factor 1 (HSF1) in mammals. However, comprehensive analyses of gene expression have revealed very large numbers of inducible genes in cells exposed to heat...
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| Veröffentlicht in: | Molecular biology of the cell 2010-01, Vol.21 (1), p.106-116 |
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| creator | Fujimoto, Mitsuaki Hayashida, Naoki Katoh, Takuma Oshima, Kouji Shinkawa, Toyohide Prakasam, Ramachandran Tan, Ke Inouye, Sachiye Takii, Ryosuke Nakai, Akira |
| description | The heat-shock response is characterized by the expression of a set of classical heat-shock genes, and is regulated by heat-shock transcription factor 1 (HSF1) in mammals. However, comprehensive analyses of gene expression have revealed very large numbers of inducible genes in cells exposed to heat shock. It is believed that HSF1 is required for the heat-inducible expression of these genes although HSF2 and HSF4 modulate some of the gene expression. Here, we identified a novel mouse HSF3 (mHSF3) translocated into the nucleus during heat shock. However, mHSF3 did not activate classical heat-shock genes such as Hsp70. Remarkably, overexpression of mHSF3 restored the expression of nonclassical heat-shock genes such as PDZK3 and PROM2 in HSF1-null mouse embryonic fibroblasts (MEFs). Although down-regulation of mHSF3 expression had no effect on gene expression or cell survival in wild-type MEF cells, it abolished the moderate expression of PDZK3 mRNA and reduced cell survival in HSF1-null MEF cells during heat shock. We propose that mHSF3 represents a unique HSF that has the potential to activate only nonclassical heat-shock genes to protect cells from detrimental stresses. |
| doi_str_mv | 10.1091/mbc.E09-07-0639 |
| format | Article |
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We propose that mHSF3 represents a unique HSF that has the potential to activate only nonclassical heat-shock genes to protect cells from detrimental stresses.</description><subject>Animals</subject><subject>Cell Nucleus - metabolism</subject><subject>Cercopithecus aethiops</subject><subject>Chickens</subject><subject>COS Cells</subject><subject>Cytoprotection</subject><subject>DNA - metabolism</subject><subject>DNA Helicases - metabolism</subject><subject>Gene Expression Regulation</subject><subject>Genome - genetics</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Heat-Shock Response - genetics</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Stress, Physiological</subject><subject>Temperature</subject><subject>Transcription Factors - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUctOxDAMjBCI95kbyo1TIGmSprkgIbQLSEgcgHNIU3dbaJulya7E35N9iIcvtsbjseVB6IzRS0Y1u-pLdzmhmlBFaM71DjpkmmsiZJHvpppKTZjMxAE6CuGdUiZErvbRAdNFnkp5iN5u8OCX0OHeLwLg--cpx40NODaA5z7CEFvb4eixdbFd2giJPrjOhtC61GjARhIa7z7wDAYIuFqM7TBb43iNn6C92nYBTrf5GL1OJy-39-Tx6e7h9uaROMlFJJZl0pWyynRFpZRlltlKOVqIoshzlhJTAmgGWrq6rOuqqvMUUBZFVoMQJT9G1xvd-aLsoXLp8tF2Zj62vR2_jLet-d8Z2sbM_NJkBWWK8iRwsRUY_ecCQjR9Gxx0nR0g_cYozlX6G1eJebVhutGHMEL9s4VRs7LFJFsMUG2oMitb0sT53-N--Vsf-DdhEIrk</recordid><startdate>20100101</startdate><enddate>20100101</enddate><creator>Fujimoto, Mitsuaki</creator><creator>Hayashida, Naoki</creator><creator>Katoh, Takuma</creator><creator>Oshima, Kouji</creator><creator>Shinkawa, Toyohide</creator><creator>Prakasam, Ramachandran</creator><creator>Tan, Ke</creator><creator>Inouye, Sachiye</creator><creator>Takii, Ryosuke</creator><creator>Nakai, Akira</creator><general>The American Society for Cell Biology</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20100101</creationdate><title>A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock</title><author>Fujimoto, Mitsuaki ; 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| ispartof | Molecular biology of the cell, 2010-01, Vol.21 (1), p.106-116 |
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| subjects | Animals Cell Nucleus - metabolism Cercopithecus aethiops Chickens COS Cells Cytoprotection DNA - metabolism DNA Helicases - metabolism Gene Expression Regulation Genome - genetics Heat-Shock Proteins - metabolism Heat-Shock Response - genetics HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Humans Mice Molecular Sequence Data Multigene Family - genetics Nuclear Proteins - metabolism Protein Binding Protein Transport Stress, Physiological Temperature Transcription Factors - metabolism |
| title | A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock |
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