Interplay between in vitro acetylation and phosphorylation of tailless HMGB1 protein.
The postsynthetic acetylation of HMGB1 protein and its truncated form affects significantly its properties as "architectural" factor - recognition of bent DNA and bending of short DNA fragments. We created mutants at the target sites (lysines 2 and 81) in the tailless HMGB1 modified by the histone acetyltransferase CBP. The results show that there is no preferential site for the enzymatic activity of CBP and both lysine moieties are modified independently. Our findings for the first time demonstrate the link between the acetylation and phosphorylation of HMGB1DeltaC in vitro. The PKC phosphorylation prior to acetylation inhibits the CBP activity 40-60% for the truncated form and its mutants. The effect of the CBP acetylation on the phosphorylation level turns out to be much more prominent. In the case of HMGB1DeltaC modified at Lys 2 and Lys 81 prior to PKC treatment background phosphorylation is detected. If only one of the lysines is modified the inhibitory effect decreases.
Pelovsky
Petar
P
Institute of Molecular Biology, Bulgarian Academy of Sciences, Acad G.Bonchev str. bld.21, 1113 Sofia, Bulgaria.
Pashev
Iliya G
IG
Pasheva
Evdokia
E
D000107:Acetylation; D000818:Animals; D024243:HMGB1 Protein / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion
D024243:HMGB1 Protein; D011994:Recombinant Proteins; D051548:Histone Acetyltransferases; D008239:Lysine