Phosphorylation of mammalian DNA topoisomerase I and activation by protein kinase C
The influence of mammalian DNA topoisomerase I phosphorylation on enzyme activity has been investigated. Dephosphorylation by calf intestine alkaline phosphatase abolished the DNA relaxing activity of DNA topoisomerase I and the sensitivity of the enzyme to its specific inhibitor, camptothecin. DNA...
Gespeichert in:
Veröffentlicht in: | The Journal of biological chemistry 1990-06, Vol.265 (16), p.9418-9422 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 9422 |
---|---|
container_issue | 16 |
container_start_page | 9418 |
container_title | The Journal of biological chemistry |
container_volume | 265 |
creator | POMMIER, Y KERRIGAN, D HARTMAN, K. D GLAZER, R. I |
description | The influence of mammalian DNA topoisomerase I phosphorylation on enzyme activity has been investigated. Dephosphorylation
by calf intestine alkaline phosphatase abolished the DNA relaxing activity of DNA topoisomerase I and the sensitivity of the
enzyme to its specific inhibitor, camptothecin. DNA topoisomerase I could be reactivated by incubation with purified protein
kinase C. DNA topoisomerase I was then able to relax supercoiled DNA processively, like the native enzyme, and to cleave 32P-end-labeled
SV40 DNA fragments at the same sequences as the native enzyme in the presence of camptothecin. These results show that active
DNA topoisomerase I is a phosphoprotein and suggest a possible regulatory role of protein kinase on topoisomerase I activity
and on its sensitivity to camptothecin. |
doi_str_mv | 10.1016/s0021-9258(19)38865-9 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79795164</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>15635558</sourcerecordid><originalsourceid>FETCH-LOGICAL-c506t-7b1ae0909a3e32498e13833783cd054ca4b82c4e52d8374dc08c1d4361c0c9bc3</originalsourceid><addsrcrecordid>eNqFkE1LxDAQhoMoun78BCEgih6qmSZpk-OyfoKooIK3kKZZG22bNekq--9t3UWP5pLDPDPvzIPQPpBTIJCdRUJSSGTKxTHIEypExhO5hkZABE0oh5d1NPpFttB2jG-kf0zCJtpMISMylyP0-FD5OKt8WNS6c77Ffoob3TS6drrF53dj3PmZd9E3Nuho8Q3WbYm16dznki8WeBZ8Z12L3107IJNdtDHVdbR7q38HPV9ePE2uk9v7q5vJ-DYxnGRdkhegLZFEamppyqSwQAWluaCmJJwZzQqRGmZ5Wgqas9IQYaBkNANDjCwM3UFHy7n9Ah9zGzvVuGhsXevW-nlUeX8hh4z9CwLPKOdc9CBfgib4GIOdqllwjQ4LBUQN1tXjoFQNShVI9WNdyb5vfxUwLxpb_natNPf1w1VdR6PradCtcfFvuEwzwemw6MGSq9xr9eWCVYXzprKNSvucPl4yEPQbMU2VVg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15635558</pqid></control><display><type>article</type><title>Phosphorylation of mammalian DNA topoisomerase I and activation by protein kinase C</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>POMMIER, Y ; KERRIGAN, D ; HARTMAN, K. D ; GLAZER, R. I</creator><creatorcontrib>POMMIER, Y ; KERRIGAN, D ; HARTMAN, K. D ; GLAZER, R. I</creatorcontrib><description>The influence of mammalian DNA topoisomerase I phosphorylation on enzyme activity has been investigated. Dephosphorylation
by calf intestine alkaline phosphatase abolished the DNA relaxing activity of DNA topoisomerase I and the sensitivity of the
enzyme to its specific inhibitor, camptothecin. DNA topoisomerase I could be reactivated by incubation with purified protein
kinase C. DNA topoisomerase I was then able to relax supercoiled DNA processively, like the native enzyme, and to cleave 32P-end-labeled
SV40 DNA fragments at the same sequences as the native enzyme in the presence of camptothecin. These results show that active
DNA topoisomerase I is a phosphoprotein and suggest a possible regulatory role of protein kinase on topoisomerase I activity
and on its sensitivity to camptothecin.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)38865-9</identifier><identifier>PMID: 2160979</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Alkaline Phosphatase - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Camptothecin - pharmacology ; Cattle ; Cell Line ; CHO cells ; Cricetinae ; DNA Topoisomerases, Type I - isolation & purification ; DNA Topoisomerases, Type I - metabolism ; DNA, Superhelical - metabolism ; Enzyme Activation ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Intestines - enzymology ; Isomerases ; Molecular Weight ; Phosphorylation ; protein kinase C ; Protein Kinase C - metabolism ; Topoisomerase I Inhibitors</subject><ispartof>The Journal of biological chemistry, 1990-06, Vol.265 (16), p.9418-9422</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-7b1ae0909a3e32498e13833783cd054ca4b82c4e52d8374dc08c1d4361c0c9bc3</citedby><cites>FETCH-LOGICAL-c506t-7b1ae0909a3e32498e13833783cd054ca4b82c4e52d8374dc08c1d4361c0c9bc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19268534$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2160979$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>POMMIER, Y</creatorcontrib><creatorcontrib>KERRIGAN, D</creatorcontrib><creatorcontrib>HARTMAN, K. D</creatorcontrib><creatorcontrib>GLAZER, R. I</creatorcontrib><title>Phosphorylation of mammalian DNA topoisomerase I and activation by protein kinase C</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The influence of mammalian DNA topoisomerase I phosphorylation on enzyme activity has been investigated. Dephosphorylation
by calf intestine alkaline phosphatase abolished the DNA relaxing activity of DNA topoisomerase I and the sensitivity of the
enzyme to its specific inhibitor, camptothecin. DNA topoisomerase I could be reactivated by incubation with purified protein
kinase C. DNA topoisomerase I was then able to relax supercoiled DNA processively, like the native enzyme, and to cleave 32P-end-labeled
SV40 DNA fragments at the same sequences as the native enzyme in the presence of camptothecin. These results show that active
DNA topoisomerase I is a phosphoprotein and suggest a possible regulatory role of protein kinase on topoisomerase I activity
and on its sensitivity to camptothecin.</description><subject>Alkaline Phosphatase - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Camptothecin - pharmacology</subject><subject>Cattle</subject><subject>Cell Line</subject><subject>CHO cells</subject><subject>Cricetinae</subject><subject>DNA Topoisomerases, Type I - isolation & purification</subject><subject>DNA Topoisomerases, Type I - metabolism</subject><subject>DNA, Superhelical - metabolism</subject><subject>Enzyme Activation</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intestines - enzymology</subject><subject>Isomerases</subject><subject>Molecular Weight</subject><subject>Phosphorylation</subject><subject>protein kinase C</subject><subject>Protein Kinase C - metabolism</subject><subject>Topoisomerase I Inhibitors</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMoun78BCEgih6qmSZpk-OyfoKooIK3kKZZG22bNekq--9t3UWP5pLDPDPvzIPQPpBTIJCdRUJSSGTKxTHIEypExhO5hkZABE0oh5d1NPpFttB2jG-kf0zCJtpMISMylyP0-FD5OKt8WNS6c77Ffoob3TS6drrF53dj3PmZd9E3Nuho8Q3WbYm16dznki8WeBZ8Z12L3107IJNdtDHVdbR7q38HPV9ePE2uk9v7q5vJ-DYxnGRdkhegLZFEamppyqSwQAWluaCmJJwZzQqRGmZ5Wgqas9IQYaBkNANDjCwM3UFHy7n9Ah9zGzvVuGhsXevW-nlUeX8hh4z9CwLPKOdc9CBfgib4GIOdqllwjQ4LBUQN1tXjoFQNShVI9WNdyb5vfxUwLxpb_natNPf1w1VdR6PradCtcfFvuEwzwemw6MGSq9xr9eWCVYXzprKNSvucPl4yEPQbMU2VVg</recordid><startdate>19900605</startdate><enddate>19900605</enddate><creator>POMMIER, Y</creator><creator>KERRIGAN, D</creator><creator>HARTMAN, K. D</creator><creator>GLAZER, R. I</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19900605</creationdate><title>Phosphorylation of mammalian DNA topoisomerase I and activation by protein kinase C</title><author>POMMIER, Y ; KERRIGAN, D ; HARTMAN, K. D ; GLAZER, R. I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-7b1ae0909a3e32498e13833783cd054ca4b82c4e52d8374dc08c1d4361c0c9bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Alkaline Phosphatase - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Camptothecin - pharmacology</topic><topic>Cattle</topic><topic>Cell Line</topic><topic>CHO cells</topic><topic>Cricetinae</topic><topic>DNA Topoisomerases, Type I - isolation & purification</topic><topic>DNA Topoisomerases, Type I - metabolism</topic><topic>DNA, Superhelical - metabolism</topic><topic>Enzyme Activation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intestines - enzymology</topic><topic>Isomerases</topic><topic>Molecular Weight</topic><topic>Phosphorylation</topic><topic>protein kinase C</topic><topic>Protein Kinase C - metabolism</topic><topic>Topoisomerase I Inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>POMMIER, Y</creatorcontrib><creatorcontrib>KERRIGAN, D</creatorcontrib><creatorcontrib>HARTMAN, K. D</creatorcontrib><creatorcontrib>GLAZER, R. I</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>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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>POMMIER, Y</au><au>KERRIGAN, D</au><au>HARTMAN, K. D</au><au>GLAZER, R. I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of mammalian DNA topoisomerase I and activation by protein kinase C</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-06-05</date><risdate>1990</risdate><volume>265</volume><issue>16</issue><spage>9418</spage><epage>9422</epage><pages>9418-9422</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The influence of mammalian DNA topoisomerase I phosphorylation on enzyme activity has been investigated. Dephosphorylation
by calf intestine alkaline phosphatase abolished the DNA relaxing activity of DNA topoisomerase I and the sensitivity of the
enzyme to its specific inhibitor, camptothecin. DNA topoisomerase I could be reactivated by incubation with purified protein
kinase C. DNA topoisomerase I was then able to relax supercoiled DNA processively, like the native enzyme, and to cleave 32P-end-labeled
SV40 DNA fragments at the same sequences as the native enzyme in the presence of camptothecin. These results show that active
DNA topoisomerase I is a phosphoprotein and suggest a possible regulatory role of protein kinase on topoisomerase I activity
and on its sensitivity to camptothecin.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2160979</pmid><doi>10.1016/s0021-9258(19)38865-9</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9258 |
ispartof | The Journal of biological chemistry, 1990-06, Vol.265 (16), p.9418-9422 |
issn | 0021-9258 1083-351X |
language | eng |
recordid | cdi_proquest_miscellaneous_79795164 |
source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | Alkaline Phosphatase - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Camptothecin - pharmacology Cattle Cell Line CHO cells Cricetinae DNA Topoisomerases, Type I - isolation & purification DNA Topoisomerases, Type I - metabolism DNA, Superhelical - metabolism Enzyme Activation Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Intestines - enzymology Isomerases Molecular Weight Phosphorylation protein kinase C Protein Kinase C - metabolism Topoisomerase I Inhibitors |
title | Phosphorylation of mammalian DNA topoisomerase I and activation by protein kinase C |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T00%3A53%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Phosphorylation%20of%20mammalian%20DNA%20topoisomerase%20I%20and%20activation%20by%20protein%20kinase%20C&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=POMMIER,%20Y&rft.date=1990-06-05&rft.volume=265&rft.issue=16&rft.spage=9418&rft.epage=9422&rft.pages=9418-9422&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/s0021-9258(19)38865-9&rft_dat=%3Cproquest_cross%3E15635558%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15635558&rft_id=info:pmid/2160979&rfr_iscdi=true |