Identification of Fkh1 and Fkh2 binding site variants associated with dynamically bound DNA elements including replication origins
| Autor: | A. Zachary Ostrow, Oscar M. Aparicio |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Cell Cycle Proteins Replication Origin FOX proteins Biology Origin of replication DNA replication foci DNA-binding protein 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Transcription (biology) Binding site DNA Fungal DNA motif Genetics genome architecture Binding Sites Base Sequence Extra View Chromatin binding Forkhead Transcription Factors chromatin binding Cell Biology Chromatin 030104 developmental biology chemistry Origin recognition complex Fox proteins 030217 neurology & neurosurgery DNA Protein Binding |
| Zdroj: | Nucleus |
| ISSN: | 1949-1042 1949-1034 |
| DOI: | 10.1080/19491034.2017.1380139 |
| Popis: | Forkhead Box (Fox) DNA binding proteins control multiple genome activities, including transcription, replication, and repair. These activities are organized spatially and temporally in the nucleus, and Fox proteins Fkh1 and Fkh2 have emerged as regulators of long-range chromosomal interactions involved with these activities, such as the clustering of replication origins programmed for early initiation. Fkh1 and Fkh2 bind a subset of replication origins and are thought to dimerize to mediate long-range chromosomal contacts between these origins. The binding of Fkh1 and/or Fkh2 (Fkh1/2) to replication origins and the recombination enhancer (RE), which is involved in DNA repair required for mating-type switching, is cell cycle-regulated and thus appears to be more dynamic than Fkh1/2 binding at regulated target genes. Here we report the identification of Fkh1/2 binding sequence variants at replication origins and the RE compared with Fkh1/2 binding sequences found at target genes of the CLB2 group. These different binding sequences have previously been characterized as weak and strong, respectively, suggesting that the presence of weak sites contributes to more dynamic interactions at replication origins and RE, possibly facilitated by Fkh1/2 dimerization and cooperative interactions with accessory proteins. We discuss the wealth of regulatory potential imbued in these features of the DNA and its binding proteins. |
| Databáze: | OpenAIRE |
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