The N-terminus of Spt16 anchors FACT to MCM2-7 for parental histone recycling.

Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE

Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.

Histones*/metabolism ; Saccharomyces cerevisiae Proteins*/metabolism ; Transcriptional Elongation Factors*/metabolism; Chromatin/genetics ; DNA Helicases/genetics ; Histone Chaperones/genetics ; Histone Chaperones/metabolism ; Molecular Chaperones/genetics ; Nucleosomes/genetics ; Multiprotein Complexes/metabolism

Parental histone recycling is vital for maintaining chromatin-based epigenetic information during replication, yet its underlying mechanisms remain unclear. Here, we uncover an unexpected role of histone chaperone FACT and its N-terminus of the Spt16 subunit during parental histone recycling and transfer in budding yeast. Depletion of Spt16 and mutations at its middle domain that impair histone binding compromise parental histone recycling on both the leading and lagging strands of DNA replication forks. Intriguingly, deletion of the Spt16-N domain impairs parental histone recycling, with a more pronounced defect observed on the lagging strand. Mechanistically, the Spt16-N domain interacts with the replicative helicase MCM2-7 and facilitates the formation of a ternary complex involving FACT, histone H3/H4 and Mcm2 histone binding domain, critical for the recycling and transfer of parental histones to lagging strands. Lack of the Spt16-N domain weakens the FACT-MCM interaction and reduces parental histone recycling. We propose that the Spt16-N domain acts as a protein-protein interaction module, enabling FACT to function as a shuttle chaperone in collaboration with Mcm2 and potentially other replisome components for efficient local parental histone recycling and inheritance.
(© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.)

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2019YFA0508900 National Key Research and Development Program; 31830048 National Natural Science Foundation of China; BJJWZYJH01201910001005 Beijing Outstanding Young Scientist Program

0 (Chromatin)
EC 3.6.4.- (DNA Helicases)
0 (Histone Chaperones)
0 (Histones)
0 (Molecular Chaperones)
0 (Nucleosomes)
0 (Saccharomyces cerevisiae Proteins)
0 (Transcriptional Elongation Factors)
0 (SPT16 protein, S cerevisiae)
0 (FACT protein, S cerevisiae)
0 (Multiprotein Complexes)

Date Created: 20231018 Date Completed: 20231201 Latest Revision: 20231210

20231215

PMC10681723

10.1093/nar/gkad846

37850662