Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C
The site-specific phosphorylation of bovine histone H1 by protein kinase C was investigated in order to further elucidate the substrate specificity of protein kinase C. Protein kinase C was found to phosphorylate histone H1 to 1 mol per mol. Using N-bromosuccinimide and thrombin digestions, the phos...
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| Veröffentlicht in: | FEBS letters 1988-07, Vol.234 (1), p.31-34 |
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| creator | Jakes, Scott Hastings, Teresa G. Reimann, Erwin M. Schlender, Keith K. |
| description | The site-specific phosphorylation of bovine histone H1 by protein kinase C was investigated in order to further elucidate the substrate specificity of protein kinase C. Protein kinase C was found to phosphorylate histone H1 to 1 mol per mol. Using
N-bromosuccinimide and thrombin digestions, the phosphorylation site was localized to the globular region of the protein, containing residues 71–122. A tryptic peptide containing the phosphorylation site was purified. Modification of the phosphoserine followed by amino acid sequence analysis demonstrated that protein kinase C phosphorylated histone H1 on serine 103. This sequence, Gly
97-Thr-Gly-Ala-Ser-Gly-Ser(PO
4)-Phe-Lys
105, supports the contention that basic amino acid residues C-terminal to the phosphorylation site are sufficient determinants for phosphorylation by protein kinase C. |
| doi_str_mv | 10.1016/0014-5793(88)81296-1 |
| format | Article |
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N-bromosuccinimide and thrombin digestions, the phosphorylation site was localized to the globular region of the protein, containing residues 71–122. A tryptic peptide containing the phosphorylation site was purified. Modification of the phosphoserine followed by amino acid sequence analysis demonstrated that protein kinase C phosphorylated histone H1 on serine 103. This sequence, Gly
97-Thr-Gly-Ala-Ser-Gly-Ser(PO
4)-Phe-Lys
105, supports the contention that basic amino acid residues C-terminal to the phosphorylation site are sufficient determinants for phosphorylation by protein kinase C.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(88)81296-1</identifier><identifier>PMID: 3134256</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Bromosuccinimide - metabolism ; Cattle ; Chromatography, High Pressure Liquid ; Fundamental and applied biological sciences. Psychology ; Histone H1 ; histones ; Histones - metabolism ; Holoproteins ; Molecular Sequence Data ; Nuclear proteins ; Phosphorylation ; Phosphorylation site ; Phosphoserine - metabolism ; Protein kinase C ; Protein Kinase C - metabolism ; Proteins ; Rats ; Serine - analogs & derivatives ; Substrate Specificity ; Thrombin - metabolism</subject><ispartof>FEBS letters, 1988-07, Vol.234 (1), p.31-34</ispartof><rights>1988</rights><rights>FEBS Letters 234 (1988) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5261-ad5d756a9eedaec148147a0a1649ad13a440e31f5f251d56e5af7b71be05ee513</citedby><cites>FETCH-LOGICAL-c5261-ad5d756a9eedaec148147a0a1649ad13a440e31f5f251d56e5af7b71be05ee513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(88)81296-1$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7184192$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3134256$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jakes, Scott</creatorcontrib><creatorcontrib>Hastings, Teresa G.</creatorcontrib><creatorcontrib>Reimann, Erwin M.</creatorcontrib><creatorcontrib>Schlender, Keith K.</creatorcontrib><title>Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The site-specific phosphorylation of bovine histone H1 by protein kinase C was investigated in order to further elucidate the substrate specificity of protein kinase C. Protein kinase C was found to phosphorylate histone H1 to 1 mol per mol. Using
N-bromosuccinimide and thrombin digestions, the phosphorylation site was localized to the globular region of the protein, containing residues 71–122. A tryptic peptide containing the phosphorylation site was purified. Modification of the phosphoserine followed by amino acid sequence analysis demonstrated that protein kinase C phosphorylated histone H1 on serine 103. This sequence, Gly
97-Thr-Gly-Ala-Ser-Gly-Ser(PO
4)-Phe-Lys
105, supports the contention that basic amino acid residues C-terminal to the phosphorylation site are sufficient determinants for phosphorylation by protein kinase C.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bromosuccinimide - metabolism</subject><subject>Cattle</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Histone H1</subject><subject>histones</subject><subject>Histones - metabolism</subject><subject>Holoproteins</subject><subject>Molecular Sequence Data</subject><subject>Nuclear proteins</subject><subject>Phosphorylation</subject><subject>Phosphorylation site</subject><subject>Phosphoserine - metabolism</subject><subject>Protein kinase C</subject><subject>Protein Kinase C - metabolism</subject><subject>Proteins</subject><subject>Rats</subject><subject>Serine - analogs & derivatives</subject><subject>Substrate Specificity</subject><subject>Thrombin - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE9vEzEQxa0KVELpNyiSDwjBYcGz_ruXShA1tFIlLnCrZDn2rOJ2s5vaG1C-Pd4mzRE4WJbf_Pxm5hFyAewTMFCfGQNRSd3wD8Z8NFA3qoITMgOjecWFMi_I7Ii8Iq9zvmflbaA5JaccuKilmpG7m4D9GNvo3RiHng4tHVdIN6shTwdT7JEmzDFskcaermIehyJdwzOTdp0bMdDljm7SMGKBHmLvMtL5G_KydV3G88N9Rn4urn7Mr6vb799u5l9uKy9rBZULMmipXIMYHHoQBoR2zIESjQvAnRAMObSyrSUEqVC6Vi81LJFJRAn8jLzf-5YBHreYR7uO2WPXuR6Hbbba8LK4Yf8EQTLDFNcFFHvQpyHnhK3dpLh2aWeB2Sl9O0Vrp2itMfYpfTsN8vbgv12uMRw_HeIu9XeHusvedW1yvY_5iGkwApq6YIs99jt2uPuv1nZx9bWeCpNuzJM6zXO5N8KS_q-IyWYfsfcYYkI_2jDEvy_0B0xItCg</recordid><startdate>19880704</startdate><enddate>19880704</enddate><creator>Jakes, Scott</creator><creator>Hastings, Teresa G.</creator><creator>Reimann, Erwin M.</creator><creator>Schlender, Keith K.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19880704</creationdate><title>Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C</title><author>Jakes, Scott ; Hastings, Teresa G. ; Reimann, Erwin M. ; Schlender, Keith K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5261-ad5d756a9eedaec148147a0a1649ad13a440e31f5f251d56e5af7b71be05ee513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bromosuccinimide - metabolism</topic><topic>Cattle</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Histone H1</topic><topic>histones</topic><topic>Histones - metabolism</topic><topic>Holoproteins</topic><topic>Molecular Sequence Data</topic><topic>Nuclear proteins</topic><topic>Phosphorylation</topic><topic>Phosphorylation site</topic><topic>Phosphoserine - metabolism</topic><topic>Protein kinase C</topic><topic>Protein Kinase C - metabolism</topic><topic>Proteins</topic><topic>Rats</topic><topic>Serine - analogs & derivatives</topic><topic>Substrate Specificity</topic><topic>Thrombin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jakes, Scott</creatorcontrib><creatorcontrib>Hastings, Teresa G.</creatorcontrib><creatorcontrib>Reimann, Erwin M.</creatorcontrib><creatorcontrib>Schlender, Keith K.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jakes, Scott</au><au>Hastings, Teresa G.</au><au>Reimann, Erwin M.</au><au>Schlender, Keith K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1988-07-04</date><risdate>1988</risdate><volume>234</volume><issue>1</issue><spage>31</spage><epage>34</epage><pages>31-34</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>The site-specific phosphorylation of bovine histone H1 by protein kinase C was investigated in order to further elucidate the substrate specificity of protein kinase C. Protein kinase C was found to phosphorylate histone H1 to 1 mol per mol. Using
N-bromosuccinimide and thrombin digestions, the phosphorylation site was localized to the globular region of the protein, containing residues 71–122. A tryptic peptide containing the phosphorylation site was purified. Modification of the phosphoserine followed by amino acid sequence analysis demonstrated that protein kinase C phosphorylated histone H1 on serine 103. This sequence, Gly
97-Thr-Gly-Ala-Ser-Gly-Ser(PO
4)-Phe-Lys
105, supports the contention that basic amino acid residues C-terminal to the phosphorylation site are sufficient determinants for phosphorylation by protein kinase C.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>3134256</pmid><doi>10.1016/0014-5793(88)81296-1</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | FEBS letters, 1988-07, Vol.234 (1), p.31-34 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78301880 |
| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Bromosuccinimide - metabolism Cattle Chromatography, High Pressure Liquid Fundamental and applied biological sciences. Psychology Histone H1 histones Histones - metabolism Holoproteins Molecular Sequence Data Nuclear proteins Phosphorylation Phosphorylation site Phosphoserine - metabolism Protein kinase C Protein Kinase C - metabolism Proteins Rats Serine - analogs & derivatives Substrate Specificity Thrombin - metabolism |
| title | Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C |
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