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4ass

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TubR bound to tubC - 26 bp - from Bacillus thuringiensis serovar israelensis pBtoxis

Structural highlights

4ass is a 11 chain structure with sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 7Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TUBR_BACTI A DNA-binding protein that is part of the type III plasmid partition system used to ensure correct segregation of the pBtoxis plasmid. Cooperatively binds to the centromere-like site (tubC), which may seed filament formation by the TubZ polymerizing GTPase, stabilizing TubZ filaments. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell (PubMed:20534443, PubMed:23010931, PubMed:25825718). Required for plasmid replication (PubMed:16936050, PubMed:17873046). Negatively regulates levels of TubZ; its effect on RNA expression has not been shown (Probable). Specifically binds iterons, 12-bp imperfect direct repeats that function as a plasmid origin of replication (PubMed:17873046, PubMed:23010931, PubMed:25825718). Four TubR dimers bind to tubC, forming an extended bent DNA-protein filament with protein wrapping helically around the outside of the DNA (PubMed:20534443, PubMed:23010931).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Bacterial plasmid partitioning systems segregate plasmids into each daughter cell. In the well-understood ParMRC plasmid partitioning system, adapter protein ParR binds to centromere parC, forming a helix around which the DNA is externally wrapped. This complex stabilizes the growth of a filament of actin-like ParM protein, which pushes the plasmids to the poles. The TubZRC plasmid partitioning system consists of two proteins, tubulin-like TubZ and TubR, and a DNA centromere, tubC, which perform analogous roles to those in ParMRC, despite being unrelated in sequence and structure. We have dissected in detail the binding sites that comprise Bacillus thuringiensis tubC, visualized the TubRC complex by electron microscopy, and determined a crystal structure of TubR bound to the tubC repeat. We show that the TubRC complex takes the form of a flexible DNA-protein filament, formed by lateral coating along the plasmid from tubC, the full length of which is required for the successful in vitro stabilization of TubZ filaments. We also show that TubR from Bacillus megaterium forms a helical superstructure resembling that of ParR. We suggest that the TubRC DNA-protein filament may bind to, and stabilize, the TubZ filament by forming such a ring-like structure around it. The helical superstructure of this TubRC may indicate convergent evolution between the actin-containing ParMRC and tubulin-containing TubZRC systems.

Superstructure of the centromeric complex of TubZRC plasmid partitioning systems.,Aylett CH, Lowe J Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16522-7. doi:, 10.1073/pnas.1210899109. Epub 2012 Sep 25. PMID:23010931^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tang M, Bideshi DK, Park HW, Federici BA. Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis. Appl Environ Microbiol. 2006 Nov;72(11):6948-54. PMID:16936050 doi:10.1128/AEM.00976-06
↑ Tang M, Bideshi DK, Park HW, Federici BA. Iteron-binding ORF157 and FtsZ-like ORF156 proteins encoded by pBtoxis play a role in its replication in Bacillus thuringiensis subsp. israelensis. J Bacteriol. 2007 Nov;189(22):8053-8. PMID:17873046 doi:10.1128/JB.00908-07
↑ Ni L, Xu W, Kumaraswami M, Schumacher MA. Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition. Proc Natl Acad Sci U S A. 2010 Jun 4. PMID:20534443
↑ Aylett CH, Lowe J. Superstructure of the centromeric complex of TubZRC plasmid partitioning systems. Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16522-7. doi:, 10.1073/pnas.1210899109. Epub 2012 Sep 25. PMID:23010931 doi:http://dx.doi.org/10.1073/pnas.1210899109
↑ Fink G, Löwe J. Reconstitution of a prokaryotic minus end-tracking system using TubRC centromeric complexes and tubulin-like protein TubZ filaments. Proc Natl Acad Sci U S A. 2015 Apr 14;112(15):E1845-50. PMID:25825718 doi:10.1073/pnas.1423746112
↑ Larsen RA, Cusumano C, Fujioka A, Lim-Fong G, Patterson P, Pogliano J. Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis. Genes Dev. 2007 Jun 1;21(11):1340-52. PMID:17510284 doi:10.1101/gad.1546107
↑ Aylett CH, Lowe J. Superstructure of the centromeric complex of TubZRC plasmid partitioning systems. Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16522-7. doi:, 10.1073/pnas.1210899109. Epub 2012 Sep 25. PMID:23010931 doi:http://dx.doi.org/10.1073/pnas.1210899109

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ass"

Categories: Bacillus thuringiensis | Large Structures | Aylett CHS | Lowe J

@@ Line 3: / Line 3: @@
 <StructureSection load='4ass' size='340' side='right'caption='[[4ass]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ass]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ASS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ASS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ass]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ASS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ASS FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4asn|4asn]], [[4aso|4aso]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ass FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ass OCA], [http://pdbe.org/4ass PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ass RCSB], [http://www.ebi.ac.uk/pdbsum/4ass PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ass ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ass FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ass OCA], [https://pdbe.org/4ass PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ass RCSB], [https://www.ebi.ac.uk/pdbsum/4ass PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ass ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/TUBR_BACTI TUBR_BACTI] A DNA-binding protein that is part of the type III plasmid partition system used to ensure correct segregation of the pBtoxis plasmid. Cooperatively binds to the centromere-like site (tubC), which may seed filament formation by the TubZ polymerizing GTPase, stabilizing TubZ filaments. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell (PubMed:20534443, PubMed:23010931, PubMed:25825718). Required for plasmid replication (PubMed:16936050, PubMed:17873046). Negatively regulates levels of TubZ; its effect on RNA expression has not been shown (Probable). Specifically binds iterons, 12-bp imperfect direct repeats that function as a plasmid origin of replication (PubMed:17873046, PubMed:23010931, PubMed:25825718). Four TubR dimers bind to tubC, forming an extended bent DNA-protein filament with protein wrapping helically around the outside of the DNA (PubMed:20534443, PubMed:23010931).<ref>PMID:16936050</ref> <ref>PMID:17873046</ref> <ref>PMID:20534443</ref> <ref>PMID:23010931</ref> <ref>PMID:25825718</ref> <ref>PMID:17510284</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus cereus var. thuringiensis smith et al. 1952]]
+[[Category: Bacillus thuringiensis]]
-[[Category: Aylett, C H.S]]
+[[Category: Large Structures]]
-[[Category: Lowe, J]]
+[[Category: Aylett CHS]]
-[[Category: Partitioning]]
+[[Category: Lowe J]]
-[[Category: Segregation]]
-[[Category: Structural protein-dna complex]]

4ass

From Proteopedia

Current revision

TubR bound to tubC - 26 bp - from Bacillus thuringiensis serovar israelensis pBtoxis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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