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IntroductionIntroduction

Replication Terminator Protein (RTP) from Bacillus Subtilis is a protein of current scientific investigation in terms of its symmetric and asymmetric nature, its ability to bind DNA and the mechanism upon which it terminates DNA replication. Belonging to a group of Replication Terminator Proteins that are commonly found in prokaryotes (in particular within the Bacillaceae family) (Pfam); RTP is often compared to another protein with a similar intracellular function, Termination Utilisation Sequence (Tus) from E. coli. RTP has been shown to exist in both symmetric (in solution and when bound to palindromic DNA sequences) and asymmetric states (when bound to native DNA). Its structural properties have proven to be integral to its function; as it must be able to bind DNA and have polarity (despite it being a homomeric dimer) in order to specifically block DNA replication from one direction and yet be “permissive” at the other end.

The Structure of RTPThe Structure of RTP

RTP has been found to exist as a symmetric protein in solution as a homomeric dimer through crystal structure determination (Bussiere, 1995). These identical subunits/monomers each contain four α helices (α1, α2, α3, α4) and three β strands (β1, β2, β3) along with a disordered N-terminal region. When the two subunits come together and the two α4 helices align, they form the dimer with an overall rectangle shape of 66Å x 35 Å x 30 Å. The long C-terminal helices (α4) are involved three interactions: contributing to the hydrophobic core (residues 93-103), an antiparallel coiled-coil structure (the two α4 helices coming together) and the contributing to the hydrophobic core of the other monomer (residue 122). Both monomers still remain structurally similar when they form the dimer in solution. It should be noted that when in solution the flexible loop between β2 and β3 are able to assume different conformations. (Bussiere, 1995)