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Swi1 associates with chromatin through the DDT domain and recruits Swi3 to preserve genomic integrity
Journal article   Open access

Swi1 associates with chromatin through the DDT domain and recruits Swi3 to preserve genomic integrity

Chiaki Noguchi, Jordan B Rapp, Yuliya V Skorobogatko, Lauren D Bailey and Eishi Noguchi
PloS one, v 7(8), pp e43988-e43988
2012
PMID: 22952839
url
https://doi.org/10.1371/journal.pone.0043988View
Published, Version of Record (VoR) Open

Abstract

Protein Structure, Tertiary Amino Acid Sequence Chromatin - metabolism Schizosaccharomyces pombe Proteins - chemistry Humans Cell Cycle Proteins - metabolism Molecular Sequence Data DNA Replication DNA-Binding Proteins - chemistry Protein Transport Cell Cycle Proteins - chemistry DNA-Binding Proteins - metabolism Schizosaccharomyces - genetics Schizosaccharomyces - metabolism DNA, Fungal - biosynthesis Genome, Fungal - genetics Schizosaccharomyces pombe Proteins - metabolism
Swi1 and Swi3 form the replication fork protection complex and play critical roles in proper activation of the replication checkpoint and stabilization of replication forks in the fission yeast Schizosaccharomyces pombe. However, the mechanisms by which the Swi1-Swi3 complex regulates these processes are not well understood. Here, we report functional analyses of the Swi1-Swi3 complex in fission yeast. Swi1 possesses the DDT domain, a putative DNA binding domain found in a variety of chromatin remodeling factors. Consistently, the DDT domain-containing region of Swi1 interacts with DNA in vitro, and mutations in the DDT domain eliminate the association of Swi1 with chromatin in S. pombe cells. DDT domain mutations also render cells highly sensitive to S-phase stressing agents and induce strong accumulation of Rad22-DNA repair foci, indicating that the DDT domain is involved in the activity of the Swi1-Swi3 complex. Interestingly, DDT domain mutations also abolish Swi1's ability to interact with Swi3 in cells. Furthermore, we show that Swi1 is required for efficient chromatin association of Swi3 and that the Swi1 C-terminal domain directly interacts with Swi3. These results indicate that Swi1 associates with chromatin through its DDT domain and recruits Swi3 to function together as the replication fork protection complex.

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Web of Science research areas
Biochemistry & Molecular Biology
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