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Proapoptotic histone H1.2 induces CASP‐3 and ‐7 activation by forming a protein complex with CYT c , APAF‐1 and CASP‐9
Author(s) -
Ruiz-Vela Antonio,
Korsmeyer Stanley J.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.049
Subject(s) - casp , histone , apoptosome , chemistry , microbiology and biotechnology , biophysics , biology , caspase , biochemistry , protein structure , dna , apoptosis , programmed cell death , protein structure prediction
Cytochrome c (CYT c ) is a protein that employs the caspase recruitment domain (CARD)‐containing proteins APAF‐1 and CASP‐9 to activate effectors CASP‐3 and ‐7. By using affinity labeling techniques and mass spectrometry analysis, we show that histone H1.2 is a regulator of caspases upon UV irradiation. We demonstrated that histone H1.2 forms a protein complex with APAF‐1, CASP‐9 and CYT c upon UV irradiation. In cell‐free systems, we show that histone H1.2 triggers activation of CASP‐3 and ‐7 via APAF‐1 and CASP‐9. We therefore conclude that upon DNA damage histone H1.2 acts as a positive regulator of apoptosome formation.

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