User:Chloe Paul/Replication Terminator Protein: Difference between revisions

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== Introduction ==
Replication Terminator Protein (RTP) from Bacillus Subtilis is a protein of current scientific investigation in terms of its ability to bind DNA, its symmetric and asymmetric nature, 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)<ref> R.D. Finn, J. Mistry, J. Tate, P. Coggill, A. Heger, J.E. Pollington, O.L. Gavin, P. Gunesekaran, G. Ceric, K. Forslund, L. Holm, E.L. Sonnhammer, S.R. Eddy, A. Bateman The Pfam protein families database [http://pfam.sanger.ac.uk/family/PF02334#tabview=tab0] Nucleic Acids Research (2010)  Database Issue 38:D211-222</ref>, RTP is often compared to another protein with 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). The structure of RTP has been shown to be integral to it's function. RTP must be able to bind DNA (and therefore must be positively charged) and bind asymetrically (despite it being a homomeric dimer) in order to specifically block DNA replication from one direction.
Replication Terminator Protein (RTP) from Bacillus Subtilis is a protein of current scientific investigation in terms of its ability to bind DNA, its symmetric and asymmetric nature, 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)<ref> R.D. Finn, J. Mistry, J. Tate, P. Coggill, A. Heger, J.E. Pollington, O.L. Gavin, P. Gunesekaran, G. Ceric, K. Forslund, L. Holm, E.L. Sonnhammer, S.R. Eddy, A. Bateman The Pfam protein families database [http://pfam.sanger.ac.uk/family/PF02334#tabview=tab0] Nucleic Acids Research (2010)  Database Issue 38:D211-222</ref>, RTP is often compared to another protein with 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). The structure of RTP has been shown to be integral to it's function. RTP must be able to bind DNA (and therefore must be positively charged) and bind asymetrically (despite it being a homomeric dimer) in order to specifically block DNA replication from one direction.
   
   
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