ArticleThe Journal of biological chemistry2014
Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Single-Molecule Techniques for Probing the Conformation, Dynamics and Interactions of Intrinsically Disordered Proteins.Biophysics reviews · 2025Article
- Revealing an origin of temperature-dependent structural change in intrinsically disordered proteins.Biophysical journal · 2025Article
- Article
- Single-molecule imaging of genome maintenance proteins encountering specific DNA sequences and structures.DNA repair · 2023Review
- Review
- Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging.Biomolecules · 2022Review
- Regulatory Roles of the N-Terminal Intrinsically Disordered Region of Modular Src.International journal of molecular sciences · 2022Review
- Dynamics of proteins with different molecular structures under solution condition.Scientific reports · 2020Article
- Review
- The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT).Nature communications · 2019Article
- The trimeric Hef-associated nuclease HAN is a 3'→5' exonuclease and is probably involved in DNA repair.Nucleic acids research · 2018Article
- Multiplex quantitative SILAC for analysis of archaeal proteomes: a case study of oxidative stress responses.Environmental microbiology · 2018Article
- Possible function of the second RecJ-like protein in stalled replication fork repair by interacting with Hef.Scientific reports · 2017Article
- Article
- FANCM interacts with PCNA to promote replication traverse of DNA interstrand crosslinks.Nucleic acids research · 2016Article
- How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe.Intrinsically disordered proteins · 2016Article
- A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.International journal of molecular sciences · 2015Article
- Unzippers, resolvers and sensors: a structural and functional biochemistry tale of RNA helicases.International journal of molecular sciences · 2015Review
- An optimized NIntrinsically disordered proteins · 2015Article
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11 authors.
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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. 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.
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