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Genes 2017, 8(5), 136; doi:10.3390/genes8050136

The Role of the N-Terminal Domains of Bacterial Initiator DnaA in the Assembly and Regulation of the Bacterial Replication Initiation Complex

1
Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, Wroclaw 53-114, Poland
2
Department of Molecular Microbiology, Faculty of Biotechnology, University of Wrocław, ul. Joliot-Curie 14A, Wrocław 50-383, Poland
*
Author to whom correspondence should be addressed.
Academic Editor: Eishi Noguchi
Received: 23 March 2017 / Revised: 28 April 2017 / Accepted: 4 May 2017 / Published: 10 May 2017
(This article belongs to the Special Issue DNA Replication Controls)
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Abstract

The primary role of the bacterial protein DnaA is to initiate chromosomal replication. The DnaA protein binds to DNA at the origin of chromosomal replication (oriC) and assembles into a filament that unwinds double-stranded DNA. Through interaction with various other proteins, DnaA also controls the frequency and/or timing of chromosomal replication at the initiation step. Escherichia coli DnaA also recruits DnaB helicase, which is present in unwound single-stranded DNA and in turn recruits other protein machinery for replication. Additionally, DnaA regulates the expression of certain genes in E. coli and a few other species. Acting as a multifunctional factor, DnaA is composed of four domains that have distinct, mutually dependent roles. For example, C-terminal domain IV interacts with double-stranded DnaA boxes. Domain III drives ATP-dependent oligomerization, allowing the protein to form a filament that unwinds DNA and subsequently binds to and stabilizes single-stranded DNA in the initial replication bubble; this domain also interacts with multiple proteins that control oligomerization. Domain II constitutes a flexible linker between C-terminal domains III–IV and N-terminal domain I, which mediates intermolecular interactions between DnaA and binds to other proteins that affect DnaA activity and/or formation of the initiation complex. Of these four domains, the role of the N-terminus (domains I–II) in the assembly of the initiation complex is the least understood and appears to be the most species-dependent region of the protein. Thus, in this review, we focus on the function of the N-terminus of DnaA in orisome formation and the regulation of its activity in the initiation complex in different bacteria. View Full-Text
Keywords: DnaA; N-terminus of DnaA; oriC; chromosomal replication; orisome; HobA; DiaA; SirA; Hda; Dps; DnaB DnaA; N-terminus of DnaA; oriC; chromosomal replication; orisome; HobA; DiaA; SirA; Hda; Dps; DnaB
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MDPI and ACS Style

Zawilak-Pawlik, A.; Nowaczyk, M.; Zakrzewska-Czerwińska, J. The Role of the N-Terminal Domains of Bacterial Initiator DnaA in the Assembly and Regulation of the Bacterial Replication Initiation Complex. Genes 2017, 8, 136.

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