slr1641 | ATP-dependent chaperone clpB 英文名称: slr1641 | ATP-dependent chaperone clpB 总访问: 292 国产/进口: 进口 半年访问: 6 产地/品牌: agrisera 产品类别: 植物试剂 规格: AS08344 最后更新: 2024-12-5 货号: CAS 号: 参考报价: 询价 立即询价 电话咨询 ...
(DnaKJE, GroEL/ES) is able to conduct the refolding both at low temperature after protein thermal inactivation and at high temperature at which protein thermal inactivation occurs; 2nd group (ClpA,ClpB, and possibly still unknown chaperones) is unable to conduct the standard refolding (i.e. at...
ClpB is a heat-shock protein from Escherichia coli with an unknown function. We studied a possible molecular chaperone activity of ClpB in vitro. Firefly l... M Zolkiewski - 《J.biol.chem》 被引量: 212发表: 1999年 Natural osmolyte trimethylamine N-oxide corrects assembly defects of mutant ...
We found that Hsp110 is by itself a bona fide ATP-dependent unfolding chaperone that can catalyze the unfolding of stable misfolded polypeptides and thus favor the conversion of stable, high affinity misfolded substrates in to stable low affinity native products of the chaperone reaction. ...
coli mutants in which ATP-dependent proteases or the DnaK chaperone was deleted. These results suggest that the impaired growth of these E. coli mutants primarily reflect the inherent instability of MetA and, thus, the methionine supply. As further evidence, the addition of methionine recovered ...
trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication. J. Biol. Chem. 289, 32965–32976 (2014). Article CAS Google Scholar Chen, B. et al. Engagement of arginine finger to ATP triggers large conformational ...
Introduction AAA+ ATPases of the MoxR family are ubiquitous and found in all major phyla of bacteria and archaea. They are proposed to fulfil chaperone-like functions assisting the maturation or assembly of metabolic protein complexes1,2, and are often found in an operon upstream of a gene ...
ClpB protein disaggregase molecular chaperone AAA+ ATPase cryo-EM Introduction Maintaining proteostasis is essential to cell and organismal health. Although molecular chaperones assist protein folding to prevent misfolding and aggregation, the majority of stress-inducible chaperones cannot rescue stress-damage...
Presents a detailed structure-function analysis of ClpB of Escherichia coli, an ATP-dependent ring-forming chaperone that mediates the resolubilization of aggregated proteins in cooperation with the DnaK chaperone system. Individual roles of ClpB domains; Conserved motifs in oligomerization; ATP hydrolysis...
Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1 During import into isolated chloroplasts, Plsp1 was targeted to the membrane via a soluble intermediate in an ATP hydrolysis-dependent manner. Insertion of ... Endow, Joshua K.,R Singhal,DE Fernandez,... - 《...