Abstract

BackgroundDNA replication and cell cycle as well as their relationship have been extensively studied in the two model organisms E. coli and B. subtilis. By contrast, little is known about these processes in cyanobacteria, even though they are crucial to the biosphere, in utilizing solar energy to renew the oxygenic atmosphere and in producing the biomass for the food chain. Recent studies have allowed the identification of several cell division factors that are specifics to cyanobacteria. Among them, Ftn6 has been proposed to function in the recruitment of the crucial FtsZ proteins to the septum or the subsequent Z-ring assembly and possibly in chromosome segregation.ResultsIn this study, we identified an as yet undescribed domain located in the conserved N-terminal region of Ftn6. This 77 amino-acids-long domain, designated here as FND (Ftn6 N-Terminal Domain), exhibits striking sequence and structural similarities with the DNA-interacting module, listed in the PFAM database as the DnaD-like domain (pfam04271). We took advantage of the sequence similarities between FND and the DnaD-like domains to construct a homology 3D-model of the Ftn6 FND domain from the model cyanobacterium Synechocystis PCC6803. Mapping of the conserved residues exposed onto the FND surface allowed us to identify a highly conserved area that could be engaged in Ftn6-specific interactions.ConclusionOverall, similarities between FND and DnaD-like domains as well as previously reported observations on Ftn6 suggest that FND may function as a DNA-interacting module thereby providing an as yet missing link between DNA replication and cell division in cyanobacteria. Consistently, we also showed that Ftn6 is involved in tolerance to DNA damages generated by UV rays.

Highlights

  • DNA replication and cell cycle as well as their relationship have been extensively studied in the two model organisms E. coli and B. subtilis

  • DnaB could function as a membrane anchoring factor for the replication initiation machinery [5] or, together with DnaI, the functional homolog of E. coli DnaC [6], in the recruitment of the ring helicase [7]

  • We showed that Ftn6depleted cells are sensitive to DNA damages generated by UV rays

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Summary

Introduction

DNA replication and cell cycle as well as their relationship have been extensively studied in the two model organisms E. coli and B. subtilis. Replication is initiated by the highly conserved AAA+ superfamily ATPase-member DnaA that binds the oriC, inducing DNA strand melting [2,3,4]. DnaB could function as a membrane anchoring factor for the replication initiation machinery [5] or, together with DnaI, the functional homolog of E. coli DnaC [6], in the recruitment of the ring helicase [7]. DnaD interacts with both DnaA and DnaB [8,9] It exhibits DNA remodelling activity, enhancing partial melting of the DNA strands, and could, function in early steps of replication such as initiating the recruitment of the ring helicase [9,10,11,12,13,14,15]. When the replication forks reach the terminus, terC, the replication complexes are dismantled in a process involving specific termination factors [16]

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