التفاصيل البيبلوغرافية
| العنوان: |
Large Multimeric Assemblies of Nucleosome Assembly Protein and Histones Revealed by Small-angle X-ray Scattering and Electron Microscopy. |
| المؤلفون: |
Newman, Emily R.1,2, Geoff Kneale, G.1, Ravelli, Raimond B. G.3, Karuppasamy, Manikandan2,3, Nejadasl, Fatemeh Karimi3, Taylor, Ian A.4, McGeehan, John E.1 john.mcgeehan@port.ac.uk |
| المصدر: |
Journal of Biological Chemistry. 8/3/2012, Vol. 287 Issue 32, p26657-2665. 9p. |
| مصطلحات موضوعية: |
*BIOCHEMICAL research, *CHROMATIN, *X-ray scattering, *ELECTRON microscopy, *HISTONES, *MOLECULAR chaperones, *ULTRACENTRIFUGATION |
| مستخلص: |
The nucleosome assembly protein (NAP) family represents a key group of histone chaperones that are essential for cell viability. Several x-ray structures of NAP1 dimers are available; however, there are currently no structures of this ubiquitous chaperone in complex with histones. We have characterized NAP1from Xenopus laevis and reveal that it forms discrete multimers with histones H2A/H2B and H3/H4 at a stoichiometry of one NAP dimer to one histone fold dimer. These complexes have been characterized by size exclusion chromatography, analytical ultracentrifugation, multiangle laser light scattering, and small-angle x-ray scattering to reveal their oligomeric assembly states in solution. By employing single-particle cryo-electron microscopy, we visualized these complexes for the first time and show that they form heterogeneous ring-like structures, potentially acting as large scaffolds for histone assembly and exchange. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
Academic Search Index |
Full Text Finder