当前位置： SCI文献检索 > BIOCHEMISTRY期刊下所有文献 > Basic and acidic regions flanking the HMG-box domain of maize HMGB1 and HMGB5 modulate the stimulatory effect on the DNA binding of transcription factor Dof2.

Basic and acidic regions flanking the HMG-box domain of maize HMGB1 and HMGB5 modulate the stimulatory effect on the DNA binding of transcription factor Dof2.

Abstract：

:The chromatin-associated high-mobility group (HMG) proteins of the plant HMGB family are characterized by a central HMG-box domain that is flanked by a basic N-terminal and an acidic C-terminal domain. By functional interaction with certain transcription factors, HMGB proteins contribute to transcriptional regulation. Previous work has shown that the maize HMGB5 protein is markedly more efficient than other HMGB proteins in stimulating the binding of transcription factor Dof2 to DNA target sites. Here we examine the structural requirements that determine the particular efficiency of HMGB5. The HMG-box domains of HMGB1 and HMGB5 (which mediate the interaction with Dof2) promoted Dof2-DNA binding to a similar extent, indicating that the terminal domains modulate the interaction with Dof2. Analysis of full-length, truncated, and chimeric HMGB1/5 proteins revealed that the acidic C-terminal domains positively influence the stimulation of Dof2-DNA binding, while the basic N-terminal domains have a rather negative effect. In particular, the C-terminal domain of HMGB5 has a striking positive effect and may account for the efficient stimulation mediated by full-length HMGB5. Interestingly, recombinant HMGB protein variants that have a relatively low affinity for linear DNA (such as proteins lacking the basic N-terminal domain) efficiently assist Dof2-DNA binding.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Grasser M,Christensen JM,Peterhänsel C,Grasser KD

doi

10.1021/bi6024947

subject

Has Abstract

pub_date

2007-05-29 00:00:00

pages

6375-82

issue

21

eissn

0006-2960

issn

1520-4995

journal_volume

46

pub_type

杂志文章

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