Details

Autor(en) / Beteiligte

• Ishino, Sonoko
• Yamagami, Takeshi
• Kitamura, Makoto
• Kodera, Noriyuki
• Mori, Tetsuya
• Sugiyama, Shyogo
• Ando, Toshio
• Goda, Natsuko
• Tenno, Takeshi
• Hiroaki, Hidekazu
• Ishino, Yoshizumi

Titel

Multiple Interactions of the Intrinsically Disordered Region between the Helicase and Nuclease Domains of the Archaeal Hef Protein

Ist Teil von

• The Journal of biological chemistry, 2014-08, Vol.289 (31), p.21627-21639

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2014

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Hef is an archaeal protein that probably functions mainly in stalled replication fork repair. The presence of an unstructured region was predicted between the two distinct domains of the Hef protein. We analyzed the interdomain region of Thermococcus kodakarensis Hef and demonstrated its disordered structure by CD, NMR, and high speed atomic force microscopy (AFM). To investigate the functions of this intrinsically disordered region (IDR), we screened for proteins interacting with the IDR of Hef by a yeast two-hybrid method, and 10 candidate proteins were obtained. We found that PCNA1 and a RecJ-like protein specifically bind to the IDR in vitro. These results suggested that the Hef protein interacts with several different proteins that work together in the pathways downstream from stalled replication fork repair by converting the IDR structure depending on the partner protein. Background: Hef/FANCM participates in interstrand cross-link DNA repair. Results: The predicted intrinsically disordered region (IDR) in Hef was experimentally verified. Proliferating cell nuclear antigen and a RecJ-like protein interact with the IDR individually, but not simultaneously. Conclusion: The IDR in Hef interacts with multiple proteins. Significance: Hef may function in DNA repair by association of its IDR with multiple partners.