Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2 alpha (eIF-2 alpha) kinase. Evidence for multitissue expression
Reticulocytes contain an eukaryotic initiation factor-2 alpha (eIF-2 alpha) kinase that is negatively regulated by hemin. This protein kinase, which has been termed heme-regulated inhibitor and heme-controlled repressor (HCR), has a strong inhibitory effect on the initiation of protein synthesis and...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-04, Vol.269 (14), p.10201-10204 |
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| container_title | The Journal of biological chemistry |
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| creator | MELLOR, H FLOWERS, K. M KIMBALL, S. R JEFFERSON, L. S |
| description | Reticulocytes contain an eukaryotic initiation factor-2 alpha (eIF-2 alpha) kinase that is negatively regulated by hemin.
This protein kinase, which has been termed heme-regulated inhibitor and heme-controlled repressor (HCR), has a strong inhibitory
effect on the initiation of protein synthesis and plays an important role in translational control in these cells. Previous
evidence has suggested that HCR may be an erythroid-specific enzyme. As reported herein, we have cloned and characterized
the cDNA encoding an eIF-2 alpha kinase from rat brain. The predicted amino acid sequence of the kinase from rat brain shows
82% homology to rabbit reticulocyte HCR with the greatest variation concentrated in a central region of approximately 135
amino acids located between protein kinase subdomains IV and VI. We have expressed the rat brain cDNA in Escherichia coli
and have demonstrated that the recombinant enzyme is a hemin-sensitive eIF-2 alpha kinase. We have also shown that mRNA recognized
by the rat brain cDNA is expressed in a wide range of non-erythroid rat tissues at a lower but significant level compared
with reticulocytes. These findings raise the possibility of additional, uncharacterized roles for HCR in non-erythroid cells. |
| doi_str_mv | 10.1016/s0021-9258(17)34044-9 |
| format | Article |
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This protein kinase, which has been termed heme-regulated inhibitor and heme-controlled repressor (HCR), has a strong inhibitory
effect on the initiation of protein synthesis and plays an important role in translational control in these cells. Previous
evidence has suggested that HCR may be an erythroid-specific enzyme. As reported herein, we have cloned and characterized
the cDNA encoding an eIF-2 alpha kinase from rat brain. The predicted amino acid sequence of the kinase from rat brain shows
82% homology to rabbit reticulocyte HCR with the greatest variation concentrated in a central region of approximately 135
amino acids located between protein kinase subdomains IV and VI. We have expressed the rat brain cDNA in Escherichia coli
and have demonstrated that the recombinant enzyme is a hemin-sensitive eIF-2 alpha kinase. We have also shown that mRNA recognized
by the rat brain cDNA is expressed in a wide range of non-erythroid rat tissues at a lower but significant level compared
with reticulocytes. These findings raise the possibility of additional, uncharacterized roles for HCR in non-erythroid cells.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(17)34044-9</identifier><identifier>PMID: 7908290</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Base Sequence ; Biological and medical sciences ; Brain - enzymology ; Cloning, Molecular ; DNA Primers ; DNA, Complementary ; eIF-2 Kinase ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hemin - pharmacology ; Male ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases - genetics ; Rabbits ; Rats ; Rats, Sprague-Dawley ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; Transferases</subject><ispartof>The Journal of biological chemistry, 1994-04, Vol.269 (14), p.10201-10204</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-f9a2b20711e73ca2c80083426417baf28f1ba3d7cbd38214863155239f0f5bf13</citedby><cites>FETCH-LOGICAL-c506t-f9a2b20711e73ca2c80083426417baf28f1ba3d7cbd38214863155239f0f5bf13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4133905$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7908290$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MELLOR, H</creatorcontrib><creatorcontrib>FLOWERS, K. M</creatorcontrib><creatorcontrib>KIMBALL, S. R</creatorcontrib><creatorcontrib>JEFFERSON, L. S</creatorcontrib><title>Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2 alpha (eIF-2 alpha) kinase. Evidence for multitissue expression</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Reticulocytes contain an eukaryotic initiation factor-2 alpha (eIF-2 alpha) kinase that is negatively regulated by hemin.
This protein kinase, which has been termed heme-regulated inhibitor and heme-controlled repressor (HCR), has a strong inhibitory
effect on the initiation of protein synthesis and plays an important role in translational control in these cells. Previous
evidence has suggested that HCR may be an erythroid-specific enzyme. As reported herein, we have cloned and characterized
the cDNA encoding an eIF-2 alpha kinase from rat brain. The predicted amino acid sequence of the kinase from rat brain shows
82% homology to rabbit reticulocyte HCR with the greatest variation concentrated in a central region of approximately 135
amino acids located between protein kinase subdomains IV and VI. We have expressed the rat brain cDNA in Escherichia coli
and have demonstrated that the recombinant enzyme is a hemin-sensitive eIF-2 alpha kinase. We have also shown that mRNA recognized
by the rat brain cDNA is expressed in a wide range of non-erythroid rat tissues at a lower but significant level compared
with reticulocytes. These findings raise the possibility of additional, uncharacterized roles for HCR in non-erythroid cells.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Brain - enzymology</subject><subject>Cloning, Molecular</subject><subject>DNA Primers</subject><subject>DNA, Complementary</subject><subject>eIF-2 Kinase</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemin - pharmacology</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transferases</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9vFCEYh4nR1G31IzThYEx7mMrLn5nh2KytNmn0oCbeCMNAB52BFWaq9nv4fWXddT3KhZD3-f2APAidArkAAvWrTAiFSlLRnkFzzjjhvJKP0ApIyyom4PNjtDogT9Fxzl9IWVzCETpqJGmpJCv0az3G4MMd1qHHZtBJm9km_6BnHwOODpvX7y6xDSb2WyrpGQ928qHKNmQ_-3uLfSj7jnclHVNFsR43g8Zn9ub67-Ecf_VBZ3uBr-59XwotdjHhaRnnEs95sdj-2CSbcyl6hp44PWb7fL-foE_XVx_Xb6vb929u1pe3lRGknisnNe0oaQBsw4ympiXl85zWHJpOO9o66DTrG9P1rKXA25qBEJRJR5zoHLAT9HLXu0nx22LzrCafjR1HHWxcsmpKkyS1-C8IddsIKnkBxQ40KeacrFOb5CedfiogautNfdhKUVspChr1x5uSJXe6v2DpJtsfUntRZf5iP9fZ6NElHYzPB4wDY5KIf9jg74bvPlnV-WiKMUVrqYCXJ1AC7Dcthayp</recordid><startdate>19940408</startdate><enddate>19940408</enddate><creator>MELLOR, H</creator><creator>FLOWERS, K. M</creator><creator>KIMBALL, S. R</creator><creator>JEFFERSON, L. S</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19940408</creationdate><title>Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2 alpha (eIF-2 alpha) kinase. Evidence for multitissue expression</title><author>MELLOR, H ; FLOWERS, K. M ; KIMBALL, S. R ; JEFFERSON, L. S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-f9a2b20711e73ca2c80083426417baf28f1ba3d7cbd38214863155239f0f5bf13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Brain - enzymology</topic><topic>Cloning, Molecular</topic><topic>DNA Primers</topic><topic>DNA, Complementary</topic><topic>eIF-2 Kinase</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemin - pharmacology</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MELLOR, H</creatorcontrib><creatorcontrib>FLOWERS, K. M</creatorcontrib><creatorcontrib>KIMBALL, S. R</creatorcontrib><creatorcontrib>JEFFERSON, L. S</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MELLOR, H</au><au>FLOWERS, K. M</au><au>KIMBALL, S. R</au><au>JEFFERSON, L. S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2 alpha (eIF-2 alpha) kinase. Evidence for multitissue expression</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-04-08</date><risdate>1994</risdate><volume>269</volume><issue>14</issue><spage>10201</spage><epage>10204</epage><pages>10201-10204</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Reticulocytes contain an eukaryotic initiation factor-2 alpha (eIF-2 alpha) kinase that is negatively regulated by hemin.
This protein kinase, which has been termed heme-regulated inhibitor and heme-controlled repressor (HCR), has a strong inhibitory
effect on the initiation of protein synthesis and plays an important role in translational control in these cells. Previous
evidence has suggested that HCR may be an erythroid-specific enzyme. As reported herein, we have cloned and characterized
the cDNA encoding an eIF-2 alpha kinase from rat brain. The predicted amino acid sequence of the kinase from rat brain shows
82% homology to rabbit reticulocyte HCR with the greatest variation concentrated in a central region of approximately 135
amino acids located between protein kinase subdomains IV and VI. We have expressed the rat brain cDNA in Escherichia coli
and have demonstrated that the recombinant enzyme is a hemin-sensitive eIF-2 alpha kinase. We have also shown that mRNA recognized
by the rat brain cDNA is expressed in a wide range of non-erythroid rat tissues at a lower but significant level compared
with reticulocytes. These findings raise the possibility of additional, uncharacterized roles for HCR in non-erythroid cells.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7908290</pmid><doi>10.1016/s0021-9258(17)34044-9</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0021-9258 1083-351X |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Biological and medical sciences Brain - enzymology Cloning, Molecular DNA Primers DNA, Complementary eIF-2 Kinase Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hemin - pharmacology Male Molecular Sequence Data Protein-Serine-Threonine Kinases - genetics Rabbits Rats Rats, Sprague-Dawley RNA, Messenger - metabolism Sequence Homology, Amino Acid Transferases |
| title | Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2 alpha (eIF-2 alpha) kinase. Evidence for multitissue expression |
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