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

@article{Ishino2014MultipleIO,
  title={Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein.},
  author={S. Ishino and Takeshi Yamagami and Makoto Kitamura and Noriyuki Kodera and Tetsuya Mori and Shyogo Sugiyama and Toshio Ando and Natsuko Goda and Takeshi Tenno and Hidekazu Hiroaki and Yoshizumi Ishino},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 31},
  pages={21627-39}
}
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… CONTINUE READING
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Intrinsically Disordered Region of Hef/FANCM 21638 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

A. Palud, G. Henneke, +4 authors D. Flament
PLoS One 8, • 2014
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