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Subunits of the histone chaperone CAF1 also mediate assembly of protamine-based chromatin.

Cell Rep. 2013 Jul 11;4(1):59-65. Epub 2013 Jun 27
Cécile M Doyen 1 , Yuri M Moshkin , Gillian E Chalkley , Karel Bezstarosti , Jeroen A A Demmers , Christina Rathke , Renate Renkawitz-Pohl , C Peter Verrijzer
Cécile M Doyen 1 , Yuri M Moshkin , Gillian E Chalkley , Karel Bezstarosti , Jeroen A A Demmers , Christina Rathke , Renate Renkawitz-Pohl , C Peter Verrijzer
+ et al

[No authors listed]

Author information
  • 1 Department of Biochemistry, Erasmus University Medical Centre, P.O. Box 1738, 3000 DR, Rotterdam, The Netherlands.

摘要


One of the most dramatic forms of chromatin reorganization occurs during spermatogenesis, when the paternal genome is repackaged from a nucleosomal to a protamine-based structure. We assessed the role of the canonical histone chaperone CAF1 in Drosophila spermatogenesis. In this process, CAF1 does not behave as a complex, but its subunits display distinct chromatin dynamics. During histone-to-protamine replacement, CAF1-p180 dissociates from the DNA while CAF1-p75 binds and stays on as a component of sperm chromatin. Association of CAF1-p75 with the paternal genome depends on CAF1-p180 and protamines. Conversely, CAF1-p75 binds protamines and is required for their incorporation into sperm chromatin. Histone removal, however, occurs independently of CAF1 or protamines. Thus, CAF1-p180 and CAF1-p75 function in a temporal hierarchy during sperm chromatin assembly, with CAF1-p75 acting as a protamine-loading factor. These results show that CAF1 subunits mediate the assembly of two fundamentally different forms of chromatin.