Structural peculiarities of the (MHF1-MHF2)4 octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: a solution SAXS study.
MHF1 and MHF2 are histone-fold-containing FANCM-associated proteins. FANCM is a Fanconi anemia (FA) complementation group protein. We previously obtained high-resolution structures of MHF1-MHF2 (MHF) and MHF in complex with a fragment of FANCM (MHF-FANCM-F). Here, we use small angle X-ray scattering (SAXS) to investigate the solution behaviors of these protein ... complexes. In combination with crystallographic data, the results of the SAXS study reveal that a long, positively charged patch exposed on the surface of the MHF complex plays a critical role in double-stranded DNA (dsDNA) binding.
Mesh Terms:
Apoptosis Regulatory Proteins, Binding Sites, Chromatin, DNA, DNA Helicases, DNA-Binding Proteins, Gene Expression, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Protein Multimerization, Protein Structure, Tertiary, Recombinant Proteins, Scattering, Small Angle, Solutions, Static Electricity, Tumor Suppressor Proteins, X-Ray Diffraction
Apoptosis Regulatory Proteins, Binding Sites, Chromatin, DNA, DNA Helicases, DNA-Binding Proteins, Gene Expression, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Protein Multimerization, Protein Structure, Tertiary, Recombinant Proteins, Scattering, Small Angle, Solutions, Static Electricity, Tumor Suppressor Proteins, X-Ray Diffraction
FEBS Lett.
Date: Sep. 17, 2013
PubMed ID: 23886707
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