RTP and Tus: Difference between revisions

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A comparison of the Replication Terminator Protein (from ''Bacillus subtilis'') and Tus (from ''Escherichia coli'') provides an interesting insight into how proteins with vastly different structures and mechanisms of action can produce essentially identical effects in their native systems.

Looking at the structures of these two proteins, it is not immediately obvious that they would perfom the same function, specifically, to arrest the progression of the replication fork along the bacterial chromosome at specific sites (termed ''Ter'' sites). Furthermore, this arrest-mechanism functions in a polar manner in both organisms, which is perhaps surprising considering the symmetrical characteristics of both proteins. <ref>Wake, RG and King, GF (1997) A tale of two terminators: crystal structures sharpen the debate on DNA replication fork arrest mechanisms. ''Structure'' 5: 1-5.</ref>

Looking at the structures of these two proteins, it is not immediately obvious that they would perfom the same function, specifically, to arrest the progression of the replication fork along the bacterial chromosome at specific sites (termed ''Ter'' sites). Furthermore, this arrest-mechanism functions in a polar manner in both organisms, which is perhaps surprising considering the symmetrical characteristics of both proteins.<ref>Wake, RG and King, GF (1997) A tale of two terminators: crystal structures sharpen the debate on DNA replication fork arrest mechanisms. ''Structure'' 5: 1-5.</ref>

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<scene name='RTP_and_Tus/Practice_structure/7'>Arg 59, His 54 and Thr 55, and also through nonbonding contacts with Tyr 58</scene>. RTP also forms non-specific interactions at its N-terminus region. <ref>Wilce JA, Vivian JP, Hastings AF, Otting G, Folmer RHA, Duggin IG, Wake RG, Wilce MCJ (2001) Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest. ''Nature Structural Biology'' 8: 206-210.</ref>

The first crystal structure of RTP was determined in 1995 by Bussiere ''et al.'' (See figure above).<ref>Bussiere DE, Bastia D, White SW (1995) Crystal structure of the replication terminator protein from ''B. subtilis'' at 2.6 A. ''Cell'' 80(4): 651-60.</ref>. This first structure, which used a symmetric B ''Ter'' DNA homologue, suggested that the RTP exists as a symmetric homodimer. The idea that a symmetric protein structure could be responsible for an inherently polar mechanism has resulted in a series of proposed solutions and discoveries regarding the mechanism of replication fork arrest.

The first crystal structure of RTP was determined in 1995 by Bussiere ''et al.'' (See figure above).<ref>Bussiere DE, Bastia D, White SW (1995) Crystal structure of the replication terminator protein from ''B. subtilis'' at 2.6 A. ''Cell'' 80(4): 651-60.</ref> This first structure, which used a symmetric B ''Ter'' DNA homologue, suggested that the RTP exists as a symmetric homodimer. The idea that a symmetric protein structure could be responsible for an inherently polar mechanism has resulted in a series of proposed solutions and discoveries regarding the mechanism of replication fork arrest.

RTP and Tus: Difference between revisions

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@@ Line 1: / Line 1: @@
 A comparison of the Replication Terminator Protein (from ''Bacillus subtilis'') and Tus (from ''Escherichia coli'') provides an interesting insight into how proteins with vastly different structures and mechanisms of action can produce essentially identical effects in their native systems.
-Looking at the structures of these two proteins, it is not immediately obvious that they would perfom the same function, specifically, to arrest the progression of the replication fork along the bacterial chromosome at specific sites (termed ''Ter'' sites). Furthermore, this arrest-mechanism functions in a polar manner in both organisms, which is perhaps surprising considering the symmetrical characteristics of both proteins. <ref>Wake, RG and King, GF (1997) A tale of two terminators: crystal structures sharpen the debate on DNA replication fork arrest mechanisms. ''Structure'' 5: 1-5.</ref>
+Looking at the structures of these two proteins, it is not immediately obvious that they would perfom the same function, specifically, to arrest the progression of the replication fork along the bacterial chromosome at specific sites (termed ''Ter'' sites). Furthermore, this arrest-mechanism functions in a polar manner in both organisms, which is perhaps surprising considering the symmetrical characteristics of both proteins.<ref>Wake, RG and King, GF (1997) A tale of two terminators: crystal structures sharpen the debate on DNA replication fork arrest mechanisms. ''Structure'' 5: 1-5.</ref>
@@ Line 59: / Line 59: @@
 <scene name='RTP_and_Tus/Practice_structure/7'>Arg 59, His 54 and Thr 55, and also through nonbonding contacts with Tyr 58</scene>. RTP also forms non-specific interactions at its N-terminus region. <ref>Wilce JA, Vivian JP, Hastings AF, Otting G, Folmer RHA, Duggin IG, Wake RG, Wilce MCJ (2001) Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest. ''Nature Structural Biology'' 8: 206-210.</ref>
-The first crystal structure of RTP was determined in 1995 by Bussiere ''et al.'' (See figure above).<ref>Bussiere DE, Bastia D, White SW (1995) Crystal structure of the replication terminator protein from ''B. subtilis'' at 2.6 A. ''Cell'' 80(4): 651-60.</ref>. This first structure, which used a symmetric B ''Ter'' DNA homologue, suggested that the RTP exists as a symmetric homodimer. The idea that a symmetric protein structure could be responsible for an inherently polar mechanism has resulted in a series of proposed solutions and discoveries regarding the mechanism of replication fork arrest.
+The first crystal structure of RTP was determined in 1995 by Bussiere ''et al.'' (See figure above).<ref>Bussiere DE, Bastia D, White SW (1995) Crystal structure of the replication terminator protein from ''B. subtilis'' at 2.6 A. ''Cell'' 80(4): 651-60.</ref> This first structure, which used a symmetric B ''Ter'' DNA homologue, suggested that the RTP exists as a symmetric homodimer. The idea that a symmetric protein structure could be responsible for an inherently polar mechanism has resulted in a series of proposed solutions and discoveries regarding the mechanism of replication fork arrest.