Alterations in the nuclear matrix protein mass correlate with heat-induced inhibition of DNA single-strand-break repair.
The total protein mass co-isolating with the nuclear matrix or nucleoid from Chinese hamster ovary (CHO) cells was observed to increase in heated cells as a function of increasing exposure temperature between 43 degrees C and 45 degrees C or of exposure time at any temperature. The sedimentation distance of the CHO cell nucleoid in sucrose gradients increased with increasing exposure time at 45 degrees C. Both these nuclear alterations correlated in a log-linear manner with heat-induced inhibition of DNA strand break repair. A two-fold threshold increase in nuclear matrix protein mass preceded any substantial inhibition of repair of DNA single-strand breaks. When preheated cells (45 degrees C for 15 min) were incubated at 37 degrees C the nuclear matrix protein mass and nucleoid sedimentation recovered with a half-time of about 5 h, while DNA single-strand-break repair recovered with a half-time of about 2 h. When preheated cells were placed at 41 degrees C (step-down heating; SDH) a further increase was observed in the nuclear matrix protein mass and the half-time of DNA strand break repair, while nucleoid sedimentation recovered toward control values. These results implicate alterations in the protein mass of the nuclear matrix in heat-induced inhibition of repair of DNA single-strand breaks.
D000818:Animals; D034961:Antigens, Nuclear; D002460:Cell Line; D006224:Cricetinae; D004260:DNA Repair; D004277:DNA, Single-Stranded; D006358:Hot Temperature; D066298:In Vitro Techniques; D009698:Nucleoproteins
D034961:Antigens, Nuclear; D004277:DNA, Single-Stranded; D009698:Nucleoproteins