Apoptotic DNA fragmentation is not related to the phosphorylation state of histone H1
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Apoptotic DNA fragmentation is not related to the phosphorylation state of histone H1. / Goebel, Wiebke; Obermeyer, Natalie; Bleicher, Nadja; Kratzmeier, Martin; Eibl, Hans-Jörg; Doenecke, Detlef; Albig, Werner.
In: Biological chemistry, Vol. 388, No. 2, 02.2007, p. 197-206.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Apoptotic DNA fragmentation is not related to the phosphorylation state of histone H1
AU - Goebel, Wiebke
AU - Obermeyer, Natalie
AU - Bleicher, Nadja
AU - Kratzmeier, Martin
AU - Eibl, Hans-Jörg
AU - Doenecke, Detlef
AU - Albig, Werner
PY - 2007/2
Y1 - 2007/2
N2 - Changes in chromatin structure, histone phosphorylation and cleavage of DNA into nucleosome-size fragments are characteristic features of apoptosis. Since H1 histones bind to the site of DNA cleavage between nucleosomal cores, the question arises as to whether the state of H1 phosphorylation influences the rate of internucleosomal cleavage. Here, we tested the relation between DNA fragmentation and H1 phosphorylation both in cultured cells and in vitro. In Jurkat cells, hyperosmotic mannitol concentration resulted in apoptosis, including nucleosomal fragmentation, whereas apoptosis induction by increased NaCl concentration was not accompanied by DNA fragmentation. However, both treatments induced dephosphorylation of H1 histones. In contrast, treatment of Raji cells with alkylphosphocholine led to induction of apoptosis with internucleosomal fragmentation, albeit without notable histone H1 dephosphorylation. These results demonstrate that dephosphorylation of H1 histones is neither a prerequisite for nor a consequence of internucleosomal cleavage. Moreover, we observed with an in vitro assay that the known enhancing effect of H1 histones on the activity of the apoptosis-induced endonuclease DFF40 is independent of the subtype or the phosphorylation state of the linker histone.
AB - Changes in chromatin structure, histone phosphorylation and cleavage of DNA into nucleosome-size fragments are characteristic features of apoptosis. Since H1 histones bind to the site of DNA cleavage between nucleosomal cores, the question arises as to whether the state of H1 phosphorylation influences the rate of internucleosomal cleavage. Here, we tested the relation between DNA fragmentation and H1 phosphorylation both in cultured cells and in vitro. In Jurkat cells, hyperosmotic mannitol concentration resulted in apoptosis, including nucleosomal fragmentation, whereas apoptosis induction by increased NaCl concentration was not accompanied by DNA fragmentation. However, both treatments induced dephosphorylation of H1 histones. In contrast, treatment of Raji cells with alkylphosphocholine led to induction of apoptosis with internucleosomal fragmentation, albeit without notable histone H1 dephosphorylation. These results demonstrate that dephosphorylation of H1 histones is neither a prerequisite for nor a consequence of internucleosomal cleavage. Moreover, we observed with an in vitro assay that the known enhancing effect of H1 histones on the activity of the apoptosis-induced endonuclease DFF40 is independent of the subtype or the phosphorylation state of the linker histone.
KW - Apoptosis/drug effects
KW - Cell Line, Tumor
KW - DNA Fragmentation/drug effects
KW - Deoxyribonucleases/drug effects
KW - Histones/chemistry
KW - Humans
KW - Jurkat Cells/drug effects
KW - Osmotic Pressure
KW - Phosphorylation
KW - Poly-ADP-Ribose Binding Proteins
KW - Staurosporine/pharmacology
U2 - 10.1515/BC.2007.022
DO - 10.1515/BC.2007.022
M3 - SCORING: Journal article
C2 - 17261083
VL - 388
SP - 197
EP - 206
JO - BIOL CHEM
JF - BIOL CHEM
SN - 1431-6730
IS - 2
ER -
