Three-dimensional topology of the SMC2/SMC4 subcomplex from chicken condensin I revealed by cross-linking and molecular modelling
| Autor: | Damien F. Hudson, Zhuo Angel Chen, William C. Earnshaw, Juri Rappsilber, Ji Hun Kim, Dietlind L. Gerloff, Helena Barysz |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Genetic Linkage Protein Conformation Condensin Histones 0302 clinical medicine Protein structure lcsh:QH301-705.5 mass spectrometry Adenosine Triphosphatases Genetics 0303 health sciences biology SMC condensin General Neuroscience Nuclear Proteins Chromatin DNA-Binding Proteins Research Article Cohesin complex Recombinant Fusion Proteins Immunology Mitosis Chromosomes General Biochemistry Genetics and Molecular Biology Cell Line 03 medical and health sciences Condensin complex coiled-coil Animals Sister chromatids Protein Interaction Domains and Motifs Coiled-coil structure 030304 developmental biology Mass spectrometry Research SMC protein Structure lcsh:Biology (General) Multiprotein Complexes biology.protein Biophysics Chickens 030217 neurology & neurosurgery cross-linking Cross-linking |
| Zdroj: | Barysz, H, Kim, J H, Chen, Z A, Hudson, D F, Rappsilber, J, Gerloff, D L & Earnshaw, W C 2015, ' Three-dimensional topology of the SMC2/SMC4 subcomplex from chicken condensin I revealed by cross-linking and molecular modelling ', Open Biology, vol. 5, no. 2, 150005 . https://doi.org/10.1098/rsob.150005 Open Biology Open Biology, Vol 5, Iss 2 (2015) |
| Popis: | SMC proteins are essential components of three protein complexes that are important for chromosome structure and function. The cohesin complex holds replicated sister chromatids together, whereas the condensin complex has an essential role in mitotic chromosome architecture. Both are involved in interphase genome organization. SMC-containing complexes are large (more than 650 kDa for condensin) and contain long anti-parallel coiled-coils. They are thus difficult subjects for conventional crystallographic and electron cryomicroscopic studies. Here, we have used amino acid-selective cross-linking and mass spectrometry combined with structure prediction to develop a full-length molecular draft three-dimensional structure of the SMC2/SMC4 dimeric backbone of chicken condensin. We assembled homology-based molecular models of the globular heads and hinges with the lengthy coiled-coils modelled in fragments, using numerous high-confidence cross-links and accounting for potential irregularities. Our experiments reveal that isolated condensin complexes can exist with their coiled-coil segments closely apposed to one another along their lengths and define the relative spatial alignment of the two anti-parallel coils. The centres of the coiled-coils can also approach one another closely in situ in mitotic chromosomes. In addition to revealing structural information, our cross-linking data suggest that both H2A and H4 may have roles in condensin interactions with chromatin. |
| Databáze: | OpenAIRE |
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