The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit.
作者： Doug W. Chan , Susan P. Lees-Miller
关键词: Kinase activity 、 DNA-Dependent Protein Kinase Catalytic Subunit 、 MAPK14 、 Ca2+/calmodulin-dependent protein kinase 、 Biology 、 Serine/threonine-specific protein kinase 、 Casein kinase 2, alpha 1 、 Biochemistry 、 Autophosphorylation 、 DNA-PKcs
摘要: The DNA-dependent protein kinase (DNA-PK) requires for activity free ends or other discontinuities in the structure of double strand DNA. In vitro, DNA-PK phosphorylates several transcription factors and DNA-binding proteins is thought to function DNA damage recognition repair and/or transcription. Here we show that vitro undergoes autophosphorylation all three subunits (DNA-PKcs, Ku p70 p80) phosphorylation correlates with inactivation serine/threonine DNA-PK. Significantly, restored by addition purified native DNA-PKcs but not Ku, suggesting due DNA-PKcs. Our data also suggest results dissociation from Ku-DNA complex. We an important mechanism regulation activity.
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