ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics.
about
In the beginning, Escherichia coli assembled the proto-ring: an initial phase of divisionCell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJHarnessing single cell sorting to identify cell division genes and regulators in bacteriaMycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assemblyCharacterization of CrgA, a new partner of the Mycobacterium tuberculosis peptidoglycan polymerization complexesTrans-translation is essential in the human pathogen Legionella pneumophilaProteolysis-Dependent Remodeling of the Tubulin Homolog FtsZ at the Division Septum in Escherichia coli.FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpPEssential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter sppAsymmetric division and differential gene expression during a bacterial developmental program requires DivIVA.Antibiotic acyldepsipeptides activate ClpP peptidase to degrade the cell division protein FtsZBacillus subtilis SepF binds to the C-terminus of FtsZ.The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ringFliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP.Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling.The interplay of ClpXP with the cell division machinery in Escherichia coli.Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function.Pharmacological inhibition of the ClpXP protease increases bacterial susceptibility to host cathelicidin antimicrobial peptides and cell envelope-active antibiotics.Single-Cell Analysis of Growth and Cell Division of the Anaerobe Desulfovibrio vulgaris HildenboroughStructural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein.The Protease Locus of Francisella tularensis LVS Is Required for Stress Tolerance and Infection in the Mammalian Host.Trapping and identification of cellular substrates of the Staphylococcus aureus ClpC chaperoneElucidation of the role of clp protease components in circadian rhythm by genetic deletion and overexpression in cyanobacteria.Critical clamp loader processing by an essential AAA+ protease in Caulobacter crescentus.An inventory of the bacterial macromolecular components and their spatial organization.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.Cell division in CorynebacterineaeThe keepers of the ring: regulators of FtsZ assembly.Functional analysis of the cyclophilin PpiB role in bacterial cell division.Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.The Escherichia coli divisome: born to divide.ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct robust cell wall construction.Identification of ClpP substrates in Caulobacter crescentus reveals a role for regulated proteolysis in bacterial development.AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ.
P2860
Q27694716-199BBCA8-7507-4837-BAB1-DD4DE85E0089Q28364545-080F81D3-55C4-4C62-8623-053037A67A45Q28485904-0B700E16-2C31-4E0E-8C2C-88B9549CE277Q28487426-30D34798-A993-4741-B019-767551799EC0Q28487435-0AA3DE8D-73FE-4C07-AF65-7BC3CEDA2F26Q28818569-86A972A0-FB28-411A-8521-C0AF550CC336Q30397832-FECC4B0A-DB79-4258-851C-91A78A0B7A42Q30497729-22B07810-46D0-4AC0-9D5D-3858C365E0B9Q33633994-63823EDA-B8B7-4C37-9B8B-D451C6AA9FBCQ33909111-1CC2555E-0EAA-4F07-8C60-B1D9739F24B8Q34015225-3C7F34EF-182F-467C-920F-28E56E8850C3Q34221202-562D319E-132C-4ECE-93FE-0979A0DB9248Q34389510-84537D1D-0C54-4800-8677-B6D6C20F111DQ34453157-6438E1E5-8C97-4121-9CBE-5BE4DD9F96A3Q34552812-15920B0E-EB56-40BE-8B7E-CA878035744CQ35002522-26FF2EE5-1B2B-40C2-8FE2-5C95B9BFF49EQ35095779-46B05313-C3BA-42C9-A28B-813AAC46B4E0Q35145217-EA2F54C7-8B50-4DE4-9D0B-A3040156BE17Q35190227-2762938A-03AC-4A0D-B9D6-0532076B8D73Q35215971-357CA37C-02A6-459F-A091-A78D2D269583Q35805434-8B660BA4-7D64-4729-A06E-B0087410D38CQ35867517-3B039864-AE5A-4470-90C5-2733BBA0F0CFQ36352866-C0AE793B-17A2-405F-BCC3-CF23F75F8FF0Q36518380-6B364119-0B0F-4DC6-85BE-6857B9914B57Q36579510-5AB8384E-0324-420B-9B5A-7CDFE7F8C67CQ36888447-425AF59C-24E4-4450-81A2-115A9175CC59Q37253049-D153896A-56DB-4B77-B43D-9290E10956D2Q37253068-EAE57A76-4238-4B7B-9757-F53A62001702Q37318075-2494BC8F-0EF5-4052-AF57-6318C75CFAD8Q37802430-AF210999-F072-4DBB-BC9D-0E7837C0A8FBQ38086221-6EE46243-41D1-4965-91B6-6C9CCD8E97DAQ38208303-1521EF1A-DF6D-436D-AA37-7D24E698B958Q38588069-64523C6F-9269-4CBC-B271-E82D7D882BCEQ38650434-50A2CF2F-F14E-4840-8BA1-5844635799E9Q39013722-CD3B7DAF-FB90-4F62-A896-5B2ADC66B135Q39364255-C708245D-A42D-470A-8167-5733174F3C67Q39919752-C38AB714-C17B-414D-8403-9AC5FE4DBA6AQ41870751-7F07D4E8-BE92-41FE-8648-7A4440934B61Q41882698-110941E1-0318-48EF-A081-B6EE31CA43A5Q42138062-D4743F49-4945-477C-A1F4-FC4826B2D44E
P2860
ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 17 June 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
ClpXP protease degrades the cy ...... dulates FtsZ polymer dynamics.
@en
ClpXP protease degrades the cy ...... dulates FtsZ polymer dynamics.
@nl
type
label
ClpXP protease degrades the cy ...... dulates FtsZ polymer dynamics.
@en
ClpXP protease degrades the cy ...... dulates FtsZ polymer dynamics.
@nl
prefLabel
ClpXP protease degrades the cy ...... dulates FtsZ polymer dynamics.
@en
ClpXP protease degrades the cy ...... dulates FtsZ polymer dynamics.
@nl
P2093
P2860
P356
P1476
ClpXP protease degrades the cy ...... dulates FtsZ polymer dynamics.
@en
P2093
Jodi L Camberg
Joel R Hoskins
Sue Wickner
P2860
P304
10614-10619
P356
10.1073/PNAS.0904886106
P407
P577
2009-06-17T00:00:00Z