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==Overview==
==Overview==
Soj and Spo0J of the Gram-negative hyperthermophile Thermus thermophilus, belong to the conserved ParAB family of bacterial proteins implicated in, plasmid and chromosome partitioning. Spo0J binds to DNA near the, replication origin and localises at the poles following initiation of, replication. Soj oscillates in the nucleoid region in an ATP- and, Spo0J-dependent fashion. Here, we show that Soj undergoes ATP-dependent, dimerisation in solution and forms nucleoprotein filaments with DNA., Crystal structures of Soj in three nucleotide states demonstrate that the, empty and ADP-bound states are monomeric, while a hydrolysis-deficient, mutant, D44A, is capable of forming a nucleotide 'sandwich' dimer. Soj, ATPase activity is stimulated by Spo0J or the N-terminal 20 amino-acid, peptide of Spo0J. Our analysis shows that dimerisation and activation, involving a peptide containing a Lys/Arg is conserved for Soj, ParA and, MinD and their modulators Spo0J, ParB and MinE, respectively. By homology, to the nitrogenase iron protein and the GTPases Ffh/FtsY, we suggest that, Soj dimerisation and regulation represent a conserved biological switch.
Soj and Spo0J of the Gram-negative hyperthermophile Thermus thermophilus belong to the conserved ParAB family of bacterial proteins implicated in plasmid and chromosome partitioning. Spo0J binds to DNA near the replication origin and localises at the poles following initiation of replication. Soj oscillates in the nucleoid region in an ATP- and Spo0J-dependent fashion. Here, we show that Soj undergoes ATP-dependent dimerisation in solution and forms nucleoprotein filaments with DNA. Crystal structures of Soj in three nucleotide states demonstrate that the empty and ADP-bound states are monomeric, while a hydrolysis-deficient mutant, D44A, is capable of forming a nucleotide 'sandwich' dimer. Soj ATPase activity is stimulated by Spo0J or the N-terminal 20 amino-acid peptide of Spo0J. Our analysis shows that dimerisation and activation involving a peptide containing a Lys/Arg is conserved for Soj, ParA and MinD and their modulators Spo0J, ParB and MinE, respectively. By homology to the nitrogenase iron protein and the GTPases Ffh/FtsY, we suggest that Soj dimerisation and regulation represent a conserved biological switch.


==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Butler, P.J.G.]]
[[Category: Butler, P J.G.]]
[[Category: Leonard, T.A.]]
[[Category: Leonard, T A.]]
[[Category: Lowe, J.]]
[[Category: Lowe, J.]]
[[Category: ATP]]
[[Category: ATP]]
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[[Category: soj]]
[[Category: soj]]


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Revision as of 17:37, 21 February 2008

File:2bek.gif


2bek, resolution 1.8Å

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STRUCTURE OF THE BACTERIAL CHROMOSOME SEGREGATION PROTEIN SOJ

OverviewOverview

Soj and Spo0J of the Gram-negative hyperthermophile Thermus thermophilus belong to the conserved ParAB family of bacterial proteins implicated in plasmid and chromosome partitioning. Spo0J binds to DNA near the replication origin and localises at the poles following initiation of replication. Soj oscillates in the nucleoid region in an ATP- and Spo0J-dependent fashion. Here, we show that Soj undergoes ATP-dependent dimerisation in solution and forms nucleoprotein filaments with DNA. Crystal structures of Soj in three nucleotide states demonstrate that the empty and ADP-bound states are monomeric, while a hydrolysis-deficient mutant, D44A, is capable of forming a nucleotide 'sandwich' dimer. Soj ATPase activity is stimulated by Spo0J or the N-terminal 20 amino-acid peptide of Spo0J. Our analysis shows that dimerisation and activation involving a peptide containing a Lys/Arg is conserved for Soj, ParA and MinD and their modulators Spo0J, ParB and MinE, respectively. By homology to the nitrogenase iron protein and the GTPases Ffh/FtsY, we suggest that Soj dimerisation and regulation represent a conserved biological switch.

About this StructureAbout this Structure

2BEK is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch., Leonard TA, Butler PJ, Lowe J, EMBO J. 2005 Jan 26;24(2):270-82. Epub 2005 Jan 6. PMID:15635448

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