Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein

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

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

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.Weanalyzed 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.

Original languageEnglish
Pages (from-to)21627-21639
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number31
DOIs
Publication statusPublished - Aug 1 2014

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein'. Together they form a unique fingerprint.

Cite this