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) x 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) x poly(dT) is strongly dependent on its redox state. Only its oxidized form, in fact, does it bind poly(dA) x 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.

Binding of the protein disulfite isomerase isoform ERp 60 to the nuclear matrix-associated regions of DNA / Ferraro, Anna; Altieri, Fabio; Coppari, S.; Eufemi, Margherita; Chichiarelli, Silvia; Turano, Carlo. - In: JOURNAL OF CELLULAR BIOCHEMISTRY. - ISSN 0730-2312. - 72:(1999), pp. 528-539. [10.1002/(SICI)1097-4644(19990315)72:4<528::AID-JCB8>3.0.CO;2-V]

Binding of the protein disulfite isomerase isoform ERp 60 to the nuclear matrix-associated regions of DNA

FERRARO, Anna;ALTIERI, Fabio;EUFEMI, Margherita;CHICHIARELLI, Silvia;TURANO, Carlo
1999

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) x 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) x poly(dT) is strongly dependent on its redox state. Only its oxidized form, in fact, does it bind poly(dA) x 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.
1999
01 Pubblicazione su rivista::01a Articolo in rivista
Binding of the protein disulfite isomerase isoform ERp 60 to the nuclear matrix-associated regions of DNA / Ferraro, Anna; Altieri, Fabio; Coppari, S.; Eufemi, Margherita; Chichiarelli, Silvia; Turano, Carlo. - In: JOURNAL OF CELLULAR BIOCHEMISTRY. - ISSN 0730-2312. - 72:(1999), pp. 528-539. [10.1002/(SICI)1097-4644(19990315)72:4<528::AID-JCB8>3.0.CO;2-V]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/241757
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