The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.
Identifieur interne : 003051 ( Main/Exploration ); précédent : 003050; suivant : 003052The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.
Auteurs : M W Melville [États-Unis] ; W J Hansen ; B C Freeman ; W J Welch ; M G KatzeSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1997.
Descripteurs français
- KwdFr :
- Interférons (pharmacologie), Liaison aux protéines, Protein-Serine-Threonine Kinases (antagonistes et inhibiteurs), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines de répression (génétique), Protéines de répression (métabolisme), Protéines du choc thermique (isolement et purification), Protéines du choc thermique (métabolisme), Protéines du choc thermique HSP40, Protéines recombinantes (métabolisme), Réaction de choc thermique, eIF-2 Kinase.
- MESH :
- antagonistes et inhibiteurs : Protein-Serine-Threonine Kinases.
- génétique : Protein-Serine-Threonine Kinases, Protéines de répression.
- isolement et purification : Protéines du choc thermique.
- métabolisme : Protein-Serine-Threonine Kinases, Protéines de répression, Protéines du choc thermique, Protéines recombinantes.
- pharmacologie : Interférons.
- Liaison aux protéines, Protéines du choc thermique HSP40, Réaction de choc thermique, eIF-2 Kinase.
English descriptors
- KwdEn :
- HSP40 Heat-Shock Proteins, Heat-Shock Proteins (isolation & purification), Heat-Shock Proteins (metabolism), Heat-Shock Response, Interferons (pharmacology), Protein Binding, Protein-Serine-Threonine Kinases (antagonists & inhibitors), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Recombinant Proteins (metabolism), Repressor Proteins (genetics), Repressor Proteins (metabolism), eIF-2 Kinase.
- MESH :
- chemical , antagonists & inhibitors : Protein-Serine-Threonine Kinases.
- chemical , genetics : Protein-Serine-Threonine Kinases, Repressor Proteins.
- chemical , isolation & purification : Heat-Shock Proteins.
- chemical , metabolism : Heat-Shock Proteins, Protein-Serine-Threonine Kinases, Recombinant Proteins, Repressor Proteins.
- chemical , pharmacology : Interferons.
- chemical : HSP40 Heat-Shock Proteins, eIF-2 Kinase.
- Heat-Shock Response, Protein Binding.
Abstract
The interferon-induced double-stranded RNA-activated protein kinase, PKR, likely contributes to both the antiviral and the antiproliferative effects of interferon. We previously found that influenza virus avoids the translational inhibitory effects of activated PKR by activating a cellular inhibitory protein, termed P58IPK, based on its Mr of 58,000. P58IPK is a member of the tetratricopeptide family of proteins and possesses significant homology to the conserved J region of the DnaJ family of heat shock proteins. We earlier hypothesized that P58IPK was kept in an inactive state with its own inhibitor (termed I-P58IPK) in uninfected cells. We therefore attempted the purification and characterization of I-P58IPK. The following data suggest that we have identified the molecular chaperone, hsp40, as 1-P58IPK. (i) The MonoP-purified I-P58IPK protein reacted with hsp40 antibody. (ii) This preparation demonstrated high specific activity in an in vitro functional assay containing only purified recombinant and native components. (iii) Purified, recombinant hsp40 protein inhibited P58IPK in an identical in vitro assay. (iv) Finally, we demonstrate that hsp40 directly complexes with P58IPK, in vitro, suggesting the inhibition occurs through a direct interaction. Our data, taken together, provide evidence for a novel intersection between the heat shock and interferon pathways, and suggest that influenza virus regulates PKR activity through the recruitment of a cellular stress pathway.
DOI: 10.1073/pnas.94.1.97
PubMed: 8990167
Affiliations:
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Le document en format XML
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last="Freeman">B C Freeman</name></author><author><name sortKey="Welch, W J" sort="Welch, W J" uniqKey="Welch W" first="W J" last="Welch">W J Welch</name></author><author><name sortKey="Katze, M G" sort="Katze, M G" uniqKey="Katze M" first="M G" last="Katze">M G Katze</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:8990167</idno><idno type="pmid">8990167</idno><idno type="doi">10.1073/pnas.94.1.97</idno><idno type="wicri:Area/PubMed/Corpus">000A49</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A49</idno><idno type="wicri:Area/PubMed/Curation">000A46</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000A46</idno><idno type="wicri:Area/PubMed/Checkpoint">000994</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000994</idno><idno type="wicri:Area/Ncbi/Merge">001173</idno><idno 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Washington</orgName><placeName><settlement type="city">Seattle</settlement><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Hansen, W J" sort="Hansen, W J" uniqKey="Hansen W" first="W J" last="Hansen">W J Hansen</name></author><author><name sortKey="Freeman, B C" sort="Freeman, B C" uniqKey="Freeman B" first="B C" last="Freeman">B C Freeman</name></author><author><name sortKey="Welch, W J" sort="Welch, W J" uniqKey="Welch W" first="W J" last="Welch">W J Welch</name></author><author><name sortKey="Katze, M G" sort="Katze, M G" uniqKey="Katze M" first="M G" last="Katze">M G Katze</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>HSP40 Heat-Shock Proteins</term><term>Heat-Shock Proteins (isolation & purification)</term><term>Heat-Shock Proteins (metabolism)</term><term>Heat-Shock Response</term><term>Interferons (pharmacology)</term><term>Protein Binding</term><term>Protein-Serine-Threonine Kinases (antagonists & inhibitors)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Recombinant Proteins (metabolism)</term><term>Repressor Proteins (genetics)</term><term>Repressor Proteins (metabolism)</term><term>eIF-2 Kinase</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Interférons (pharmacologie)</term><term>Liaison aux protéines</term><term>Protein-Serine-Threonine Kinases (antagonistes et inhibiteurs)</term><term>Protein-Serine-Threonine Kinases (génétique)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines de répression (génétique)</term><term>Protéines de répression (métabolisme)</term><term>Protéines du choc thermique (isolement et purification)</term><term>Protéines du choc thermique (métabolisme)</term><term>Protéines du choc thermique HSP40</term><term>Protéines recombinantes (métabolisme)</term><term>Réaction de choc thermique</term><term>eIF-2 Kinase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein-Serine-Threonine Kinases</term><term>Repressor Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Heat-Shock Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Heat-Shock Proteins</term><term>Protein-Serine-Threonine Kinases</term><term>Recombinant Proteins</term><term>Repressor Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Interferons</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>HSP40 Heat-Shock Proteins</term><term>eIF-2 Kinase</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protein-Serine-Threonine Kinases</term><term>Protéines de répression</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines du choc thermique</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protein-Serine-Threonine Kinases</term><term>Protéines de répression</term><term>Protéines du choc thermique</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Interférons</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Heat-Shock Response</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Liaison aux protéines</term><term>Protéines du choc thermique HSP40</term><term>Réaction de choc thermique</term><term>eIF-2 Kinase</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The interferon-induced double-stranded RNA-activated protein kinase, PKR, likely contributes to both the antiviral and the antiproliferative effects of interferon. We previously found that influenza virus avoids the translational inhibitory effects of activated PKR by activating a cellular inhibitory protein, termed P58IPK, based on its Mr of 58,000. P58IPK is a member of the tetratricopeptide family of proteins and possesses significant homology to the conserved J region of the DnaJ family of heat shock proteins. We earlier hypothesized that P58IPK was kept in an inactive state with its own inhibitor (termed I-P58IPK) in uninfected cells. We therefore attempted the purification and characterization of I-P58IPK. The following data suggest that we have identified the molecular chaperone, hsp40, as 1-P58IPK. (i) The MonoP-purified I-P58IPK protein reacted with hsp40 antibody. (ii) This preparation demonstrated high specific activity in an in vitro functional assay containing only purified recombinant and native components. (iii) Purified, recombinant hsp40 protein inhibited P58IPK in an identical in vitro assay. (iv) Finally, we demonstrate that hsp40 directly complexes with P58IPK, in vitro, suggesting the inhibition occurs through a direct interaction. Our data, taken together, provide evidence for a novel intersection between the heat shock and interferon pathways, and suggest that influenza virus regulates PKR activity through the recruitment of a cellular stress pathway.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Washington (État)</li></region><settlement><li>Seattle</li></settlement><orgName><li>Université de Washington</li></orgName></list><tree><noCountry><name sortKey="Freeman, B C" sort="Freeman, B C" uniqKey="Freeman B" first="B C" last="Freeman">B C Freeman</name><name sortKey="Hansen, W J" sort="Hansen, W J" uniqKey="Hansen W" first="W J" last="Hansen">W J Hansen</name><name sortKey="Katze, M G" sort="Katze, M G" uniqKey="Katze M" first="M G" last="Katze">M G Katze</name><name sortKey="Welch, W J" sort="Welch, W J" uniqKey="Welch W" first="W J" last="Welch">W J Welch</name></noCountry><country name="États-Unis"><region name="Washington (État)"><name sortKey="Melville, M W" sort="Melville, M W" uniqKey="Melville M" first="M W" last="Melville">M W Melville</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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