Expression and Characterization of Human FKBP52, an Immunophilin that Associates with the 90-kDa Heat Shock Protein and is a Component of Steroid Receptor Complexes
Using an FK506 affinity column to identify mammalian immunosuppressant-binding proteins, we identified an immunophilin with an apparent Mr≈ 55,000, which we have named FKBP52. We used chemically determined peptide sequence and a computerized algorithm to search GenPept, the translated GenBank data b...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1992-11, Vol.89 (22), p.10974-10978 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Peattie, Debra A. Harding, Matthew W. Fleming, Mark A. DeCenzo, Maureen T. Lippke, Judith A. Livingston, David J. Benasutti, Matt |
| description | Using an FK506 affinity column to identify mammalian immunosuppressant-binding proteins, we identified an immunophilin with an apparent Mr≈ 55,000, which we have named FKBP52. We used chemically determined peptide sequence and a computerized algorithm to search GenPept, the translated GenBank data base, and identified two cDNAs likely to encode the murine FKBP52 homolog. We amplified a murine cDNA fragment, used it to select a human FKBP52 (hFKBP52) cDNA clone, and then used the clone to deduce the hFKBP52 sequence (calculated Mr51,810) and to express hFKBP52 in Escherichia coli. Recombinant hFKBP52 has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and an FKBP12-like consensus sequence that probably defines the immunosuppressant-binding site. FKBP52 is apparently common to several vertebrate species and associates with the 90-kDa heat shock protein (hsp90) in untransformed mammalian steroid receptor complexes. The putative immunosuppressant-binding site is probably distinct from the hsp90-binding site, and we predict that FKBP52 has different structural domains to accommodate these functions. hFKBP52 contains 12 protein kinase phosphorylation-site motifs and a potential calmodulin-binding site, implying that posttranslational phosphorylation could generate multiple isoforms of the protein and that calmodulin and intracellular Ca2+levels could affect FKBP52 function. FKBP52 transcripts are present in a variety of human tissues and could vary in abundance and/or stability. |
| doi_str_mv | 10.1073/pnas.89.22.10974 |
| format | Article |
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We used chemically determined peptide sequence and a computerized algorithm to search GenPept, the translated GenBank data base, and identified two cDNAs likely to encode the murine FKBP52 homolog. We amplified a murine cDNA fragment, used it to select a human FKBP52 (hFKBP52) cDNA clone, and then used the clone to deduce the hFKBP52 sequence (calculated Mr51,810) and to express hFKBP52 in Escherichia coli. Recombinant hFKBP52 has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and an FKBP12-like consensus sequence that probably defines the immunosuppressant-binding site. FKBP52 is apparently common to several vertebrate species and associates with the 90-kDa heat shock protein (hsp90) in untransformed mammalian steroid receptor complexes. The putative immunosuppressant-binding site is probably distinct from the hsp90-binding site, and we predict that FKBP52 has different structural domains to accommodate these functions. hFKBP52 contains 12 protein kinase phosphorylation-site motifs and a potential calmodulin-binding site, implying that posttranslational phosphorylation could generate multiple isoforms of the protein and that calmodulin and intracellular Ca2+levels could affect FKBP52 function. FKBP52 transcripts are present in a variety of human tissues and could vary in abundance and/or stability.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.89.22.10974</identifier><identifier>PMID: 1279700</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Isomerases - genetics ; Amino Acid Isomerases - isolation & purification ; Amino Acid Isomerases - metabolism ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Binding and carrier proteins ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Blotting, Northern ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; cDNA ; Cloning, Molecular ; Complementary DNA ; complex ; Escherichia coli - genetics ; expression ; FKBP52 protein ; Fundamental and applied biological sciences. Psychology ; genes ; Heat shock proteins ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - isolation & purification ; Heat-Shock Proteins - metabolism ; Humans ; Immunity (Disease) ; immunophilin ; Immunosuppressants ; Macromolecular Substances ; man ; Mice ; Molecular Sequence Data ; Molecular Weight ; nucleotide sequence ; Oligodeoxyribonucleotides ; Organ Specificity ; Peptidylprolyl Isomerase ; predictions ; Proteins ; receptors ; Receptors, Steroid - metabolism ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Regional identity ; Restriction Mapping ; RNA Probes ; Sequence Homology, Amino Acid ; Skeletal muscle ; Steroid receptors ; steroids ; Substrate specificity ; Tacrolimus - metabolism ; Transcription, Genetic</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1992-11, Vol.89 (22), p.10974-10978</ispartof><rights>Copyright 1992 The National Academy of Sciences of the United States of America</rights><rights>1993 INIST-CNRS</rights><rights>Copyright National Academy of Sciences Nov 15, 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-381f4056346c134af147f1f20d3898d2f07398b79d8ffa5c2a3ca089435cf8133</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/89/22.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2362034$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2362034$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4502083$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1279700$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Peattie, Debra A.</creatorcontrib><creatorcontrib>Harding, Matthew W.</creatorcontrib><creatorcontrib>Fleming, Mark A.</creatorcontrib><creatorcontrib>DeCenzo, Maureen T.</creatorcontrib><creatorcontrib>Lippke, Judith A.</creatorcontrib><creatorcontrib>Livingston, David J.</creatorcontrib><creatorcontrib>Benasutti, Matt</creatorcontrib><title>Expression and Characterization of Human FKBP52, an Immunophilin that Associates with the 90-kDa Heat Shock Protein and is a Component of Steroid Receptor Complexes</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Using an FK506 affinity column to identify mammalian immunosuppressant-binding proteins, we identified an immunophilin with an apparent Mr≈ 55,000, which we have named FKBP52. We used chemically determined peptide sequence and a computerized algorithm to search GenPept, the translated GenBank data base, and identified two cDNAs likely to encode the murine FKBP52 homolog. We amplified a murine cDNA fragment, used it to select a human FKBP52 (hFKBP52) cDNA clone, and then used the clone to deduce the hFKBP52 sequence (calculated Mr51,810) and to express hFKBP52 in Escherichia coli. Recombinant hFKBP52 has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and an FKBP12-like consensus sequence that probably defines the immunosuppressant-binding site. FKBP52 is apparently common to several vertebrate species and associates with the 90-kDa heat shock protein (hsp90) in untransformed mammalian steroid receptor complexes. The putative immunosuppressant-binding site is probably distinct from the hsp90-binding site, and we predict that FKBP52 has different structural domains to accommodate these functions. hFKBP52 contains 12 protein kinase phosphorylation-site motifs and a potential calmodulin-binding site, implying that posttranslational phosphorylation could generate multiple isoforms of the protein and that calmodulin and intracellular Ca2+levels could affect FKBP52 function. FKBP52 transcripts are present in a variety of human tissues and could vary in abundance and/or stability.</description><subject>Amino Acid Isomerases - genetics</subject><subject>Amino Acid Isomerases - isolation & purification</subject><subject>Amino Acid Isomerases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Binding and carrier proteins</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>cDNA</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>complex</subject><subject>Escherichia coli - genetics</subject><subject>expression</subject><subject>FKBP52 protein</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Heat shock proteins</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - isolation & purification</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Immunity (Disease)</subject><subject>immunophilin</subject><subject>Immunosuppressants</subject><subject>Macromolecular Substances</subject><subject>man</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>nucleotide sequence</subject><subject>Oligodeoxyribonucleotides</subject><subject>Organ Specificity</subject><subject>Peptidylprolyl Isomerase</subject><subject>predictions</subject><subject>Proteins</subject><subject>receptors</subject><subject>Receptors, Steroid - metabolism</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Regional identity</subject><subject>Restriction Mapping</subject><subject>RNA Probes</subject><subject>Sequence Homology, Amino Acid</subject><subject>Skeletal muscle</subject><subject>Steroid receptors</subject><subject>steroids</subject><subject>Substrate specificity</subject><subject>Tacrolimus - metabolism</subject><subject>Transcription, Genetic</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkk1v1DAQhiMEKkvhzgGEhSrEgSz-SuJIXMrSshWVqCicLdexibeJHWyHLvwefihOd1kKBziN7PcZv-OZybKHCM4RrMjLwYowZ_Uc43SuK3orm6WI8pLW8HY2gxBXOaOY3s3uhbCCENYFg3vZHsJVXUE4y34crQevQjDOAmEbsGiFFzIqb76LOF06DZZjLyw4fvf6rMAvEgVO-n60bmhNZyyIrYjgMAQnjYgqgCsT23SpQA3zyzcCLFXSz1snL8GZd1GZjZEJQICF6wdnlY2TzXlydaYBH5RUQ3T-Wu3UWoX72R0tuqAebON-9un46ONimZ--f3uyODzNZVHQmBOGNIVFSWgpEaFCI1pppDFsCKtZg3XqWM0uqrphWotCYkGkgKympJCaIUL2s1ebd4fxoleNTIV50fHBm174b9wJw_9UrGn5Z_eVF5CWRUp_tk337suoQuS9CVJ1nbDKjYFXhEBKKvxfEJWEMAxRAp_-Ba7c6G3qAU8yJmm-02twA0nvQvBK7wpGkE9bwqct4azmGPPrLUkpj29-9HfCZi2SfrDVRZCi015YacIOowXEkE39er7FJoNf6g0jrseui2odE_rk32giHm2IVUjD3yGYlBgSSn4CX1znxg</recordid><startdate>19921115</startdate><enddate>19921115</enddate><creator>Peattie, Debra A.</creator><creator>Harding, Matthew W.</creator><creator>Fleming, Mark A.</creator><creator>DeCenzo, Maureen T.</creator><creator>Lippke, Judith A.</creator><creator>Livingston, David J.</creator><creator>Benasutti, Matt</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>IQODW</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7T3</scope><scope>M81</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19921115</creationdate><title>Expression and Characterization of Human FKBP52, an Immunophilin that Associates with the 90-kDa Heat Shock Protein and is a Component of Steroid Receptor Complexes</title><author>Peattie, Debra A. ; Harding, Matthew W. ; Fleming, Mark A. ; DeCenzo, Maureen T. ; Lippke, Judith A. ; Livingston, David J. ; Benasutti, Matt</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c554t-381f4056346c134af147f1f20d3898d2f07398b79d8ffa5c2a3ca089435cf8133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Isomerases - genetics</topic><topic>Amino Acid Isomerases - isolation & purification</topic><topic>Amino Acid Isomerases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Binding and carrier proteins</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>cDNA</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>complex</topic><topic>Escherichia coli - genetics</topic><topic>expression</topic><topic>FKBP52 protein</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Heat shock proteins</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - isolation & purification</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Immunity (Disease)</topic><topic>immunophilin</topic><topic>Immunosuppressants</topic><topic>Macromolecular Substances</topic><topic>man</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>nucleotide sequence</topic><topic>Oligodeoxyribonucleotides</topic><topic>Organ Specificity</topic><topic>Peptidylprolyl Isomerase</topic><topic>predictions</topic><topic>Proteins</topic><topic>receptors</topic><topic>Receptors, Steroid - metabolism</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Regional identity</topic><topic>Restriction Mapping</topic><topic>RNA Probes</topic><topic>Sequence Homology, Amino Acid</topic><topic>Skeletal muscle</topic><topic>Steroid receptors</topic><topic>steroids</topic><topic>Substrate specificity</topic><topic>Tacrolimus - metabolism</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Peattie, Debra A.</creatorcontrib><creatorcontrib>Harding, Matthew W.</creatorcontrib><creatorcontrib>Fleming, Mark A.</creatorcontrib><creatorcontrib>DeCenzo, Maureen T.</creatorcontrib><creatorcontrib>Lippke, Judith A.</creatorcontrib><creatorcontrib>Livingston, David J.</creatorcontrib><creatorcontrib>Benasutti, Matt</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Human Genome Abstracts</collection><collection>Biochemistry Abstracts 3</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Peattie, Debra A.</au><au>Harding, Matthew W.</au><au>Fleming, Mark A.</au><au>DeCenzo, Maureen T.</au><au>Lippke, Judith A.</au><au>Livingston, David J.</au><au>Benasutti, Matt</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and Characterization of Human FKBP52, an Immunophilin that Associates with the 90-kDa Heat Shock Protein and is a Component of Steroid Receptor Complexes</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1992-11-15</date><risdate>1992</risdate><volume>89</volume><issue>22</issue><spage>10974</spage><epage>10978</epage><pages>10974-10978</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Using an FK506 affinity column to identify mammalian immunosuppressant-binding proteins, we identified an immunophilin with an apparent Mr≈ 55,000, which we have named FKBP52. We used chemically determined peptide sequence and a computerized algorithm to search GenPept, the translated GenBank data base, and identified two cDNAs likely to encode the murine FKBP52 homolog. We amplified a murine cDNA fragment, used it to select a human FKBP52 (hFKBP52) cDNA clone, and then used the clone to deduce the hFKBP52 sequence (calculated Mr51,810) and to express hFKBP52 in Escherichia coli. Recombinant hFKBP52 has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and an FKBP12-like consensus sequence that probably defines the immunosuppressant-binding site. FKBP52 is apparently common to several vertebrate species and associates with the 90-kDa heat shock protein (hsp90) in untransformed mammalian steroid receptor complexes. The putative immunosuppressant-binding site is probably distinct from the hsp90-binding site, and we predict that FKBP52 has different structural domains to accommodate these functions. hFKBP52 contains 12 protein kinase phosphorylation-site motifs and a potential calmodulin-binding site, implying that posttranslational phosphorylation could generate multiple isoforms of the protein and that calmodulin and intracellular Ca2+levels could affect FKBP52 function. FKBP52 transcripts are present in a variety of human tissues and could vary in abundance and/or stability.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1279700</pmid><doi>10.1073/pnas.89.22.10974</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1992-11, Vol.89 (22), p.10974-10978 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_4502083 |
| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Isomerases - genetics Amino Acid Isomerases - isolation & purification Amino Acid Isomerases - metabolism Amino Acid Sequence Analytical, structural and metabolic biochemistry Base Sequence Binding and carrier proteins Binding Sites Biochemistry Biological and medical sciences Blotting, Northern Carrier Proteins - genetics Carrier Proteins - isolation & purification Carrier Proteins - metabolism cDNA Cloning, Molecular Complementary DNA complex Escherichia coli - genetics expression FKBP52 protein Fundamental and applied biological sciences. Psychology genes Heat shock proteins Heat-Shock Proteins - genetics Heat-Shock Proteins - isolation & purification Heat-Shock Proteins - metabolism Humans Immunity (Disease) immunophilin Immunosuppressants Macromolecular Substances man Mice Molecular Sequence Data Molecular Weight nucleotide sequence Oligodeoxyribonucleotides Organ Specificity Peptidylprolyl Isomerase predictions Proteins receptors Receptors, Steroid - metabolism Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Regional identity Restriction Mapping RNA Probes Sequence Homology, Amino Acid Skeletal muscle Steroid receptors steroids Substrate specificity Tacrolimus - metabolism Transcription, Genetic |
| title | Expression and Characterization of Human FKBP52, an Immunophilin that Associates with the 90-kDa Heat Shock Protein and is a Component of Steroid Receptor Complexes |
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