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Two Forms of the Nuclear Matrix–Bound p53 Protein in HEK293 Cells
Author(s) -
LAPSHINA MARIA A.,
PARKHOMENKO IGOR I.,
TERENTIEV ALEXEI A.
Publication year - 2006
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1378.019
Subject(s) - nuclear matrix , hek 293 cells , chemistry , nuclear protein , suppressor , alkali metal , matrix (chemical analysis) , transcription factor , transcription (linguistics) , biophysics , biochemistry , biology , dna , gene , chromatography , organic chemistry , linguistics , philosophy , chromatin
Like many other transcription factors, the tumor suppressor protein p53 is bound to the nuclear matrix (NM). To study the interaction of p53 with the NM in more detail, we used alkaline and acidic extractions of NM proteins. It was found that there are two forms of p53, alkali‐ and acid‐soluble, in NM of HEK293 cells and only one alkali‐soluble form in NM of actinomycin D–treated MCF‐7 cells. We suggest that distinct forms of p53 differ either in interactions with NM proteins or in their charges.