Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA

Protein ERp60, previously found in the internal nuclear matrix in chicken liver nuclei, is a member of the protein disulfide isomerase family. It binds DNA and double helical polynucleotides in vitro with a preferential recognition toward the matrix‐associated regions of DNA and poly(dA)·poly(dT), a...

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Veröffentlicht in:Journal of cellular biochemistry 1999-03, Vol.72 (4), p.528-539
Hauptverfasser: Ferraro, Anna, Altieri, Fabio, Coppari, Sabina, Eufemi, Margherita, Chichiarelli, Silvia, Turano, Carlo
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container_end_page 539
container_issue 4
container_start_page 528
container_title Journal of cellular biochemistry
container_volume 72
creator Ferraro, Anna
Altieri, Fabio
Coppari, Sabina
Eufemi, Margherita
Chichiarelli, Silvia
Turano, Carlo
description Protein ERp60, previously found in the internal nuclear matrix in chicken liver nuclei, is a member of the protein disulfide isomerase family. It binds DNA and double helical polynucleotides in vitro with a preferential recognition toward the matrix‐associated regions of DNA and poly(dA)·poly(dT), and its binding is inhibited by distamycin. ERp60 can be cross‐linked chemically to DNA in the intact nuclei, suggesting that its association with DNA is present in vivo. As a whole, these results indicate that ERp60 is a component of the subset of nuclear matrix proteins that are responsible for the attachment of DNA to the nuclear matrix and for the formation of DNA loops. A distinctive feature of this protein, which has two thioredoxin‐like sites, is that its affinity to poly(dA)·poly(dT) is strongly dependent on its redox state. Only its oxidized form, in fact, does it bind poly(dA)·poly(dT). The hypothesis can be made that through the intervention of ERp60, the redox state of the nucleus influences the formation or the stability of some selected nuclear matrix–DNA interactions. J. Cell. Biochem. 72:528–539, 1999. © 1999 Wiley‐Liss, Inc.
doi_str_mv 10.1002/(SICI)1097-4644(19990315)72:4<528::AID-JCB8>3.0.CO;2-V
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It binds DNA and double helical polynucleotides in vitro with a preferential recognition toward the matrix‐associated regions of DNA and poly(dA)·poly(dT), and its binding is inhibited by distamycin. ERp60 can be cross‐linked chemically to DNA in the intact nuclei, suggesting that its association with DNA is present in vivo. As a whole, these results indicate that ERp60 is a component of the subset of nuclear matrix proteins that are responsible for the attachment of DNA to the nuclear matrix and for the formation of DNA loops. A distinctive feature of this protein, which has two thioredoxin‐like sites, is that its affinity to poly(dA)·poly(dT) is strongly dependent on its redox state. Only its oxidized form, in fact, does it bind poly(dA)·poly(dT). The hypothesis can be made that through the intervention of ERp60, the redox state of the nucleus influences the formation or the stability of some selected nuclear matrix–DNA interactions. J. Cell. Biochem. 72:528–539, 1999. © 1999 Wiley‐Liss, Inc.</description><identifier>ISSN: 0730-2312</identifier><identifier>EISSN: 1097-4644</identifier><identifier>DOI: 10.1002/(SICI)1097-4644(19990315)72:4&lt;528::AID-JCB8&gt;3.0.CO;2-V</identifier><identifier>PMID: 10022612</identifier><language>eng</language><publisher>New York: John Wiley &amp; Sons, Inc</publisher><subject>Animals ; chicken liver nuclei ; Chickens ; Cross-Linking Reagents - metabolism ; Distamycins - pharmacology ; DNA-Binding Proteins - metabolism ; DNA-protein interaction ; Heat-Shock Proteins - metabolism ; Isoenzymes - metabolism ; Isomerases - metabolism ; Liver - enzymology ; Nuclear Matrix - enzymology ; Nuclear Proteins - metabolism ; nuclear scaffold attachment regions ; Oxidation-Reduction ; Poly dA-dT - metabolism ; protein disulfide isomerase ; Protein Disulfide-Isomerases - metabolism ; Thioredoxins - chemistry</subject><ispartof>Journal of cellular biochemistry, 1999-03, Vol.72 (4), p.528-539</ispartof><rights>Copyright © 1999 Wiley‐Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4038-d9143b7303a3b2fd0ac559eaee262f700b9bfcb7044a5c6c32f21324d035dc23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F%28SICI%291097-4644%2819990315%2972%3A4%3C528%3A%3AAID-JCB8%3E3.0.CO%3B2-V$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F%28SICI%291097-4644%2819990315%2972%3A4%3C528%3A%3AAID-JCB8%3E3.0.CO%3B2-V$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10022612$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ferraro, Anna</creatorcontrib><creatorcontrib>Altieri, Fabio</creatorcontrib><creatorcontrib>Coppari, Sabina</creatorcontrib><creatorcontrib>Eufemi, Margherita</creatorcontrib><creatorcontrib>Chichiarelli, Silvia</creatorcontrib><creatorcontrib>Turano, Carlo</creatorcontrib><title>Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA</title><title>Journal of cellular biochemistry</title><addtitle>J. Cell. Biochem</addtitle><description>Protein ERp60, previously found in the internal nuclear matrix in chicken liver nuclei, is a member of the protein disulfide isomerase family. It binds DNA and double helical polynucleotides in vitro with a preferential recognition toward the matrix‐associated regions of DNA and poly(dA)·poly(dT), and its binding is inhibited by distamycin. ERp60 can be cross‐linked chemically to DNA in the intact nuclei, suggesting that its association with DNA is present in vivo. As a whole, these results indicate that ERp60 is a component of the subset of nuclear matrix proteins that are responsible for the attachment of DNA to the nuclear matrix and for the formation of DNA loops. A distinctive feature of this protein, which has two thioredoxin‐like sites, is that its affinity to poly(dA)·poly(dT) is strongly dependent on its redox state. Only its oxidized form, in fact, does it bind poly(dA)·poly(dT). 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Cell. Biochem</addtitle><date>1999-03-15</date><risdate>1999</risdate><volume>72</volume><issue>4</issue><spage>528</spage><epage>539</epage><pages>528-539</pages><issn>0730-2312</issn><eissn>1097-4644</eissn><abstract>Protein ERp60, previously found in the internal nuclear matrix in chicken liver nuclei, is a member of the protein disulfide isomerase family. It binds DNA and double helical polynucleotides in vitro with a preferential recognition toward the matrix‐associated regions of DNA and poly(dA)·poly(dT), and its binding is inhibited by distamycin. ERp60 can be cross‐linked chemically to DNA in the intact nuclei, suggesting that its association with DNA is present in vivo. As a whole, these results indicate that ERp60 is a component of the subset of nuclear matrix proteins that are responsible for the attachment of DNA to the nuclear matrix and for the formation of DNA loops. A distinctive feature of this protein, which has two thioredoxin‐like sites, is that its affinity to poly(dA)·poly(dT) is strongly dependent on its redox state. Only its oxidized form, in fact, does it bind poly(dA)·poly(dT). The hypothesis can be made that through the intervention of ERp60, the redox state of the nucleus influences the formation or the stability of some selected nuclear matrix–DNA interactions. J. Cell. Biochem. 72:528–539, 1999. © 1999 Wiley‐Liss, Inc.</abstract><cop>New York</cop><pub>John Wiley &amp; Sons, Inc</pub><pmid>10022612</pmid><doi>10.1002/(SICI)1097-4644(19990315)72:4&lt;528::AID-JCB8&gt;3.0.CO;2-V</doi><tpages>12</tpages></addata></record>
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subjects Animals
chicken liver nuclei
Chickens
Cross-Linking Reagents - metabolism
Distamycins - pharmacology
DNA-Binding Proteins - metabolism
DNA-protein interaction
Heat-Shock Proteins - metabolism
Isoenzymes - metabolism
Isomerases - metabolism
Liver - enzymology
Nuclear Matrix - enzymology
Nuclear Proteins - metabolism
nuclear scaffold attachment regions
Oxidation-Reduction
Poly dA-dT - metabolism
protein disulfide isomerase
Protein Disulfide-Isomerases - metabolism
Thioredoxins - chemistry
title Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA
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