Abstract：
:DciA is a newly discovered bacterial protein involved in loading the replicative helicase DnaB onto DNA at the initiation step of chromosome replication. Its three-dimensional structure is composed of a folded N-terminal domain (residues 1-111) resembling K Homology domains and a long disordered C-terminal tail (residues 112-157) which structure-activity relationship remains to be elucidated. In the present study on Vibrio cholerae DciA, we emphasize the importance of its disordered region to load DnaB onto DNA using surface plasmon resonance (SPR) and isothermal titration microcalorimetry (ITC). Then we characterize the conformational ensemble of the full-length protein using a combination of circular dichroism (CD), small angle X-ray scattering (SAXS), and molecular dynamics (MD) simulations. The atomic-level structural ensemble generated by MD simulations is in very good agreement with SAXS data. From initial conformations of the C-terminal tail without any secondary structure, our simulations bring to light several transient helical structures in this segment, which might be molecular recognition features (MoRFs) for the binding to DnaB and its recruitment and loading onto DNA.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Chan-Yao-Chong M,Marsin S,Quevillon-Cheruel S,Durand D,Ha-Duong Tdoi
10.1016/j.jsb.2020.107573subject
Has Abstractpub_date
2020-10-01 00:00:00pages
107573issue
1eissn
1047-8477issn
1095-8657pii
S1047-8477(20)30146-5journal_volume
212pub_type
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journal_title：Journal of structural biology
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