File:Steps_in_nucleosome_assembly.svg
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Summary
DescriptionSteps in nucleosome assembly.svg |
English: Nucleosome assembly begins with the binding of acetylated histone H3–H4 complexes to the assembly factor CAF-1. This complex is then recruited to the replication fork by an interaction with the sliding clamp, and a tetramer of histones H3 and H4 is loaded onto the nascent DNA to form half of a new nucleosome. Dimers of histones H2A and H2B are then loaded onto the DNA, probably with the assistance of other assembly factors such as NAP-1, to form the complete histone octamer. Chromatin-remodeling complexes contribute to nucleosome assembly and spacing. The number of histone H3 and H4 subunits that interact with CAF-1 is not clear. These subunits form highly stable tetramers in solution (unlike histones H2A and H2B, which form dimers) and it is therefore thought that CAF-1 loads a complete H3–H4 tetramer as shown here. There is some evidence, however, that CAF-1 can interact with an H3–H4 dimer, in which case the loading of a tetramer would require two CAF-1–histone complexes.[1] |
Date | |
Source | The Cell Cycle. Principles of Control. |
Author | David O Morgan |
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1 January 2007
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current | 18:03, 1 May 2020 | 512 × 488 (307 KB) | Rob Hurt | Uploaded a work by David O Morgan from The Cell Cycle. Principles of Control. with UploadWizard |
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