The Coiled-Coil of the Human Rad50 DNA Repair Protein Contains Specific Segments of Increased Flexibility

Protein structural features are usually determined by defining regularities in a large population of homogeneous molecules. However, irregular features such as structural variation and flexibility are likely to be missed, despite their vital role for their biological function. In this paper, we repo...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 100; no. 13; pp. 7581 - 7586
Main Authors van Noort, John, van der Heijden, Thijn, de Jager, Martijn, Wyman, Claire, Kanaar, Roland, Dekker, Cees
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 24.06.2003
National Acad Sciences
SeriesFrom the Cover
Subjects
Adenosine triphosphatases
Amino acids
Bending
Biological Sciences
Biophysical Phenomena
Biophysics
Curvature
Deoxyribonucleic acid
DNA
DNA - analysis
DNA Repair
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Humans
Imaging
Microscopy, Atomic Force
Models, Molecular
Models, Statistical
Molecules
Polymers
Protein Binding
Protein Structure, Tertiary
Proteins
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Trajectories
Zinc
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Summary:Protein structural features are usually determined by defining regularities in a large population of homogeneous molecules. However, irregular features such as structural variation and flexibility are likely to be missed, despite their vital role for their biological function. In this paper, we report the observation of striking irregularities in the flexibility of the coiled-coil region of the human Rad50 DNA repair protein. Existing methods to quantitatively analyze flexibility are applicable to homogeneous polymers only. Because protein coiled-coils cannot be assumed to be homogeneous, we develop a method to quantify the local flexibility from high-resolution atomic force microscopy images. Indeed, in Rad50 coiled-coils, two positions of increased flexibility are observed. We discuss how this dynamic structural feature is integral to Rad50 function.
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To whom correspondence should be addressed. E-mail: noort@mb.tn.tudelft.nl.
This paper was submitted directly (Track II) to the PNAS office.
Abbreviations: R/M, Rad50 and Mre11; SMC, structural maintenance of chromosome; AFM, atomic force microscopy.
Edited by Nancy Kleckner, Harvard University, Cambridge, MA, and approved April 21, 2003
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1330706100