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 journalArticle

18 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

Fingerprint

Archaeal Proteins
Proteins
Thermococcus
Repair
Two-Hybrid System Techniques
Atomic Force Microscopy
Yeast
Yeasts
Atomic force microscopy
Nuclear magnetic resonance

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. / Ishino, Sonoko; Yamagami, Takeshi; Kitamura, Makoto; Kodera, Noriyuki; Mori, Tetsuya; Sugiyama, Shyogo; Ando, Toshio; Goda, Natsuko; Tenno, Takeshi; Hiroaki, Hidekazu; Ishino, Yoshizumi.

In: Journal of Biological Chemistry, Vol. 289, No. 31, 01.08.2014, p. 21627-21639.

Research output: Contribution to journalArticle

Ishino, Sonoko ; Yamagami, Takeshi ; Kitamura, Makoto ; Kodera, Noriyuki ; Mori, Tetsuya ; Sugiyama, Shyogo ; Ando, Toshio ; Goda, Natsuko ; Tenno, Takeshi ; Hiroaki, Hidekazu ; Ishino, Yoshizumi. / Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. In: Journal of Biological Chemistry. 2014 ; Vol. 289, No. 31. pp. 21627-21639.
@article{8665652c71424f138031b60689f14d48,
title = "Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein",
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.",
author = "Sonoko 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",
year = "2014",
month = "8",
day = "1",
doi = "10.1074/jbc.M114.554998",
language = "English",
volume = "289",
pages = "21627--21639",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "31",

}

TY - JOUR

T1 - Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein

AU - Ishino, Sonoko

AU - Yamagami, Takeshi

AU - Kitamura, Makoto

AU - Kodera, Noriyuki

AU - Mori, Tetsuya

AU - Sugiyama, Shyogo

AU - Ando, Toshio

AU - Goda, Natsuko

AU - Tenno, Takeshi

AU - Hiroaki, Hidekazu

AU - Ishino, Yoshizumi

PY - 2014/8/1

Y1 - 2014/8/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84905389211&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84905389211&partnerID=8YFLogxK

U2 - 10.1074/jbc.M114.554998

DO - 10.1074/jbc.M114.554998

M3 - Article

C2 - 24947516

AN - SCOPUS:84905389211

VL - 289

SP - 21627

EP - 21639

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 31

ER -