Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study.
about
Structure of the N-terminal fragment ofEscherichia coliLon proteaseStepwise unfolding of a β barrel protein by the AAA+ ClpXP protease.Designing specific protein-protein interactions using computation, experimental library screening, or integrated methodsModular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo.The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpPA single ClpS monomer is sufficient to direct the activity of the ClpA hexamerSpecificity versus stability in computational protein designClpXP, an ATP-powered unfolding and protein-degradation machineRemodeling of a delivery complex allows ClpS-mediated degradation of N-degron substrates.Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAPSpecificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpXSculpting the proteome with AAA(+) proteases and disassembly machines.Geobacillus thermodenitrificans YjbH recognizes the C-terminal end of Bacillus subtilis Spx to accelerate Spx proteolysis by ClpXP.Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.ATP-dependent proteases differ substantially in their ability to unfold globular proteinsUnique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpXEngineering synthetic adaptors and substrates for controlled ClpXP degradationSspB delivery of substrates for ClpXP proteolysis probed by the design of improved degradation tagsA degradation signal recognition in prokaryotes.Regulated Proteolysis in Bacteria: Caulobacter.Small-molecule control of protein degradation using split adaptors.Activation of a dormant ClpX recognition motif of bacteriophage Mu repressor by inducing high local flexibility.Selective adaptor dependent protein degradation in bacteria.Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation.Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial speciesA Phosphosignaling Adaptor Primes the AAA+ Protease ClpXP to Drive Cell Cycle-Regulated Proteolysis.Rapid depletion of target proteins allows identification of coincident physiological responses.Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone.Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates.The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer.Roles of the N-domains of the ClpA unfoldase in binding substrate proteins and in stable complex formation with the ClpP protease.Identification of New Degrons in Streptococcus mutans Reveals a Novel Strategy for Engineering Targeted, Controllable Proteolysis.Regulated Proteolysis in Bacteria.Altered tethering of the SspB adaptor to the ClpXP protease causes changes in substrate delivery.Versatile modes of peptide recognition by the AAA+ adaptor protein SspB.Binding and degradation of heterodimeric substrates by ClpAP and ClpXP.
P2860
Q27663923-406F756B-0275-40B6-A271-BF3197F45569Q30155499-1803D61D-13EF-4BF6-AD0D-8D9FAA797C99Q30416858-A6DD33AF-4507-48CB-83DA-EB5485E0F62CQ33581226-67A79B7B-6FDF-4574-9DBE-C73E3F944F1CQ33633994-46EA93EC-44B4-4C2D-9473-0B5679623AF8Q33726457-4473D8BF-0B24-48FE-9661-86037324CC4BQ33943985-0B89E0ED-D8B6-43DE-B460-6F536D29C993Q34198403-0E193AEC-8C80-40C8-8CD9-AF219FCAFFBEQ34218175-27E2DDF0-C072-4B3A-9106-BE8747EABDB9Q34304801-F7F62B3A-69E3-444B-89FB-036B9D32FF85Q35215013-3FDE9871-C4A4-4283-94CD-56F2C378EB8CQ35904074-7B1C835A-C209-4DC4-B513-4837BC88C32AQ36525721-BE2BC168-0A22-45F5-BF12-F95E9A74E688Q36933762-FBE8D6F4-8001-452D-9815-970BDA8CF882Q37254059-820BC7E5-7952-4B38-8B87-4F258BDE9D81Q37278581-7BFD970A-CCC0-4547-B62F-634EA710A5C9Q37372136-534F5F12-1949-4052-8471-AB9640FB1875Q37484390-B6F7E867-28AE-42EF-8287-7CFA3B8B9B81Q38606541-5F8C7CCD-407E-4C5E-A64A-9D3FE035457EQ39022244-D86D58B1-A4BE-4CA4-8780-8855F6BAC594Q39253018-588678A9-13EF-4439-B4E2-0EA3B38457A1Q39260728-8170B9AC-0508-40A5-8DE1-23BAC5F1A929Q39273861-21355455-2F2D-4D25-9707-AF6EDC482FD4Q40016654-2081BB4F-A89E-454B-BBE7-C036596CDF75Q40403943-4E3AD2B6-EB45-430D-9EAF-B5963A400870Q41442624-6F9BA749-C431-4208-AB1A-8F01BD1A60AFQ41584414-26DDCA46-2A8B-4275-B319-B5697F99C200Q42412455-56377CD0-A2E6-43C9-A0DB-2D3D12B9A15AQ43151994-6062AC3B-CF7E-4624-B504-8165088BC613Q45228992-B69ADF6C-CB75-490C-A423-69F4D50C8060Q46738159-A00605FF-D348-41AF-AEEC-A1C54F000CF6Q47192205-79D7B417-D667-426A-A948-A0D4BE139F8BQ52323704-16E6AAAA-2D3D-4B00-A9B6-AA4107CA2090Q54446250-936A44F3-3141-459C-BD47-CF5B01915AF2Q54486455-848AA5D2-DF7A-4B58-84D3-46EE76517218Q54494643-D823DA70-8722-4F9B-99B8-703D5B4679D9
P2860
Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Bivalent tethering of SspB to ...... ivery: a protein-design study.
@en
Bivalent tethering of SspB to ...... ivery: a protein-design study.
@nl
type
label
Bivalent tethering of SspB to ...... ivery: a protein-design study.
@en
Bivalent tethering of SspB to ...... ivery: a protein-design study.
@nl
prefLabel
Bivalent tethering of SspB to ...... ivery: a protein-design study.
@en
Bivalent tethering of SspB to ...... ivery: a protein-design study.
@nl
P2093
P1433
P1476
Bivalent tethering of SspB to ...... livery: a protein-design study
@en
P2093
David A Wah
Greg L Hersch
Tania A Baker
P304
P356
10.1016/S1097-2765(04)00027-9
P577
2004-02-01T00:00:00Z