Abstract:
:Interferon regulatory factors (IRFs) are transcription factors for interferon-related genes, which manifest both antiviral and tumor-suppressor activities and regulate cell growth in response to DNA damage. For the transcription initiation of the interferon-beta gene, IRFs form a macromolecular assembly bound to the promoter DNA, referred to as an enhancesome, together with several other transcription factors and DNA-binding proteins. The three-dimensional structure of IRF-DNA complex would provide insights into the structure and function of the enhancesome. In this study, we crystallized the DNA-binding domain of interferon regulatory factor-2 complexed with a DNA fragment. The crystals reproducibly grew by the vapor diffusion technique with 2-methyl-pentanediol from solutions containing small detergents, such as n-octyl-beta-d-glucoside. Cryocrystallographic experiments showed that crystals belong to space group P212121 with a = 90.66 Å, b = 101.01 Å, c = 171.58 Å and diffract up to 2.8 Å resolution. The absorption measurements of a solution in which the crystals were dissolved indicate that the DNA-binding domain binds to the DNA as a dimer. The calculated values of the solvent contents suggest that the protein-DNA complexes form a multimer in the crystal. These features may reflect the association of the complexes in the enhancesome. Copyright 1998 Academic Press.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Kusumoto M,Fujii Y,Tsukuda Y,Ohira T,Kyougoku Y,Taniguchi T,Hakoshima Tdoi
10.1006/jsbi.1998.3970subject
Has Abstractpub_date
1998-01-01 00:00:00pages
363-6issue
3eissn
1047-8477issn
1095-8657pii
S1047-8477(98)93970-3journal_volume
121pub_type
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