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Selected nuclear matrix proteins are targets for poly(ADP‐ribose)‐binding
Author(s) -
Malanga Maria,
Kleczkowska Hanna E.,
Althaus Felix R.
Publication year - 1998
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19980915)70:4<596::aid-jcb15>3.0.co;2-f
Subject(s) - nuclear matrix , poly adp ribose polymerase , chemistry , ribose , matrix (chemical analysis) , nuclear protein , microbiology and biotechnology , biochemistry , biology , transcription factor , dna , enzyme , chromatin , gene , chromatography , polymerase
Recent evidence suggests that poly(ADP‐ribose) may take part in DNA strand break signalling due to its ability to interact with and affect the function of specific target proteins. Using a poly(ADP‐ribose) blot assay, we have found that several nuclear matrix proteins from human and murine cells bind ADP‐ribose polymers with high affinity. The binding was observed regardless of the procedure used to isolate nuclear matrices, and it proved resistant to high salt concentrations. In murine lymphoma LY‐cell cultures, the spontaneous appearance of radiosensitive LY‐S sublines was associated with a loss of poly(ADP‐ribose)‐binding of several nuclear matrix proteins. Because of the importance of the nuclear matrix in DNA processing reactions, the targeting of matrix proteins could be an important aspect of DNA damage signalling via the poly ADP‐ribosylation system. J. Cell. Biochem. 70:596–603. © 1998 Wiley‐Liss, Inc.