Conserved Ser residues in the basic region of the bZIP-type transcription factor HBP-1a(17): importance in DNA binding and possible targets for phosphorylation

被引:26
作者
Meshi, T [1 ]
Moda, I [1 ]
Minami, M [1 ]
Okanami, M [1 ]
Iwabuchi, M [1 ]
机构
[1] Kyoto Univ, Grad Sch Sci, Dept Bot, Sakyo Ku, Kyoto 60601, Japan
关键词
bZIP; Ca2+; DNA binding; HBP1a(17); phosphorylation;
D O I
10.1023/A:1005934332530
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
HBP-1a(17) is representative of a group of plant bZIP-type transcription factors which includes HBP-1a proteins and G-box-binding factors. We found kinase activity in wheat nuclear extract that phosphorylated HBP-1a(l7). Experiments using recombinant HBP-1a(l7) derivatives as substrates revealed that all three of the Ser residues in the basic region, Ser-261, Ser-265, and Ser-269, were phosphorylated in a Ca2+-stimulated manner. DNA-binding analysis of mutants with a Ser-to-Glu change, prepared to mimic the phosphorylated proteins, indicated that introduction of a negative charge at position 265 or 269 prevents HBP-1a(l7) from binding DNA not only in the homodimer of mutants but also in heterodimers with a wild-type protein. It is therefore suggested that the phosphorylation regulates the function of HBP-1a(17) at least at the level of DNA binding. Since Ser-265 and Ser-269 are highly conserved among the plant bZIP-type factors known to date, a common Ca2+-mediated regulatory mechanism may exert an effect on the bZIP-type factors through phosphorylation of these conserved Ser residues.
引用
收藏
页码:125 / 136
页数:12
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