Replication Termination Protein: Difference between revisions
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<StructureSection load='2dpd' size='450' side='right' scene='' caption='Assymetric RTP dimer bound to the B site in a Ter region (PDB code [[2dpd]])'> | <StructureSection load='2dpd' size='450' side='right' scene='' caption='Assymetric RTP dimer bound to the B site in a Ter region (PDB code [[2dpd]])'> | ||
== Function == | == Function == | ||
[[Image:RTP.png| | [[Image:RTP.png|200px|left|thumb| Diagram of RTP monomer with secondary structure highlighted.]] | ||
The '''replication termination protein''' (RTP) is one of only two well-defined proteins known to be involved in arresting DNA replication forks, the other being a protein known as tus (termination utilisation substance) from E. coli <ref> Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morkikawa K, (1996) Structure of a replication-terminator protein complexed with DNA. Nature, 383:598-603 </ref>. RTP was discovered in ''Bacillus subtilis'' and has been identified as a DNA binding protein of the winged helix family that forms a dimer of 29kDa. This dimeric form has been shown to have an exceptionally high affinity for its cognate binding sites( Kd ~10-11M-1)<ref> Wilce et. al. (2001) Structure of the RTP−DNA complex and the mechanism of polar replication fork arrest. Nature Structural Biology, 8:206-210 </ref>, otherwise known as Termination sites (Ter sites). These Ter sites are found in multiple locations in the ''B. subtilis'' genome <ref> Gautam A. et.al. (2001) A single domain of the replication termination protein of ''Bacillus subtilis'' is involved in arresting both DnaB helicase and RNA polymerase. Journal of Biological Chemistry, 276:23471-23479</ref>. For more details see:<br /> | The '''replication termination protein''' (RTP) is one of only two well-defined proteins known to be involved in arresting DNA replication forks, the other being a protein known as tus (termination utilisation substance) from E. coli <ref> Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morkikawa K, (1996) Structure of a replication-terminator protein complexed with DNA. Nature, 383:598-603 </ref>. RTP was discovered in ''Bacillus subtilis'' and has been identified as a DNA binding protein of the winged helix family that forms a dimer of 29kDa. This dimeric form has been shown to have an exceptionally high affinity for its cognate binding sites( Kd ~10-11M-1)<ref> Wilce et. al. (2001) Structure of the RTP−DNA complex and the mechanism of polar replication fork arrest. Nature Structural Biology, 8:206-210 </ref>, otherwise known as Termination sites (Ter sites). These Ter sites are found in multiple locations in the ''B. subtilis'' genome <ref> Gautam A. et.al. (2001) A single domain of the replication termination protein of ''Bacillus subtilis'' is involved in arresting both DnaB helicase and RNA polymerase. Journal of Biological Chemistry, 276:23471-23479</ref>. For more details see:<br /> | ||
*[[RTP and Tus]]<br /> | *[[RTP and Tus]]<br /> | ||
