TY - JOUR
T1 - Stimulation of DNA-dependent protein kinase activity by high mobility group proteins 1 and 2
AU - Watanabe, Fumiaki
AU - Shirakawa, Hitoshi
AU - Yoshida, Michiteru
AU - Tsukada, Kinji
AU - Teraoka, Hirobumi
PY - 1994/7/29
Y1 - 1994/7/29
N2 - After incubation of high mobility group (HMG) proteins 1 and 2 with DNA-dependent protein kinase (DNA-PK) and [γ-32P]ATP in the presence of double-stranded DNA, not only phosphorylation of HMG proteins but also enhancement of autophosphorylation of the catalytic of 350 kDa in DNA-PK was observed. DNA-PK activity with a synthetic peptide and α-casein as substrates was stimulated several-fold by HMG1, HMG2, and the DNA-binding domains. The stimulation was decreased at higher concentrations of HMG proteins, and DNA-PK activity was inhibited by histone H1. Electrophoretic mobility shift analysis suggests that HMG proteins facilitate the binding of DNA-PK to DNA.
AB - After incubation of high mobility group (HMG) proteins 1 and 2 with DNA-dependent protein kinase (DNA-PK) and [γ-32P]ATP in the presence of double-stranded DNA, not only phosphorylation of HMG proteins but also enhancement of autophosphorylation of the catalytic of 350 kDa in DNA-PK was observed. DNA-PK activity with a synthetic peptide and α-casein as substrates was stimulated several-fold by HMG1, HMG2, and the DNA-binding domains. The stimulation was decreased at higher concentrations of HMG proteins, and DNA-PK activity was inhibited by histone H1. Electrophoretic mobility shift analysis suggests that HMG proteins facilitate the binding of DNA-PK to DNA.
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U2 - 10.1006/bbrc.1994.1992
DO - 10.1006/bbrc.1994.1992
M3 - Article
C2 - 8048945
AN - SCOPUS:0027937302
SN - 0006-291X
VL - 202
SP - 736
EP - 742
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -