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

Abstract

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.

DNA replication restart and cellular dynamics of Hef helicase/nuclease protein in Haloferax volcanii

“…In the case of TkoHef, the interaction with PCNA1 does not involve a canonical PIP motif [52], but a disordered region of Hef between the helicase and nuclease domains. Interestingly, these predicted long disordered regions connecting two catalytic domains are a common feature of euryarchaeal Hef and eukaryotic FANCM proteins [50]. So, both creanarchaeal XPF and euryarchaeal Hef proteins can interact with PCNA and display biochemical activities consistent with XPF/Hef being involved in DNA repair and/or replication restart.…”

“…Consistent with a role of Hef in replication and/or repair, Thermococcus kodakarensis Hef has recently been shown to interact with TkoPCNA1 [50]. In the cell, the replication factor PCNA (Proliferating Cell Nuclear Antigen) encircles double-strand DNA (dsDNA) and enhances e.g.…”

Two-Ball Structure of the Flagellar Hook-Length Control Protein FliK as Revealed by High-Speed Atomic Force Microscopy

“…Here, we used high-speed atomic force microscopy (HS-AFM) to examine the structure of FliK at the single molecular level and hereby to gain an insight into the hook-length control mechanism. HS-AFM is capable of visualizing protein molecules in action at high spatiotemporal resolution [16,17] and has been proven to be valid not only for ordered proteins [18][19][20][21][22] but also for ID proteins [23][24][25]. Although the NMR data suggested that FliK N would be structurally disordered, HS-AFM observation revealed that a FliK molecule in solution took on a shape of two balls linked by a flexible string and that the N-terminal ball is more stable than the C-terminal ball.…”

Disordered interdomain region of Gins is important for functional tetramer formation to stimulate MCM helicase in Thermoplasma acidophilum

“…The amino acid sequences of the IDR are generally divergent and sequence alignments do not provide any conserved sequence motif. 21) Three organisms, Thermoplasma volcanium (NP_111072), Picrophilus torridus (AAT42851), and Ferroplasma acidarmanus (YP_008141571), were found in the total genome database as close relatives of T. acidophilum (NP_394502). We made a multiple sequence alignment of the Gins51 homologs from these data and found that the interdomain regions are indeed highly divergent, in contrast to the two distinct domains.…”