Literature DB >> 25900372

Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.

Hideki Taguchi1.   

Abstract

Chaperonin GroEL is an essential chaperone that assists in protein folding in the cell. Since one GroEL ring binds one GroES heptamer, the GroEL double ring permits the formation of two types of GroEL:GroES complexes: asymmetric 1:1 "bullet"-shaped and symmetric 1:2 "football"-shaped GroEL:GroES2 complexes. There have been continuing debates about the mechanism and which complex is critical to the chaperonin-assisted folding. In this review, I summarize the recent progress on the football complex.
Copyright © 2015 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  GroEL; Hsp60; chaperone; chaperonin; protein folding

Mesh：

Substances：

Year:  2015        PMID： 25900372     DOI： 10.1016/j.jmb.2015.04.007

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


  14 in total

1.  Reconciling the controversy regarding the functional importance of bullet- and football-shaped GroE complexes.

Authors:  Lavi S Bigman; Amnon Horovitz
Journal:  J Biol Chem       Date:  2019-08-01       Impact factor: 5.157

2.  Substrate protein dependence of GroEL-GroES interaction cycle revealed by high-speed atomic force microscopy imaging.

Authors:  Daisuke Noshiro; Toshio Ando
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2018-06-19       Impact factor: 6.237

3.  Translation-coupled protein folding assay using a protease to monitor the folding status.

Authors:  Tatsuya Niwa; Eri Uemura; Yuki Matsuno; Hideki Taguchi
Journal:  Protein Sci       Date:  2019-05-03       Impact factor: 6.725

4.  Allosteric differences dictate GroEL complementation of E. coli.

Authors:  Jared Sivinski; Duc Ngo; Christopher J Zerio; Andrew J Ambrose; Edmond R Watson; Lynn K Kaneko; Marius M Kostelic; Mckayla Stevens; Anne-Marie Ray; Yangshin Park; Chunxiang Wu; Michael T Marty; Quyen Q Hoang; Donna D Zhang; Gabriel C Lander; Steven M Johnson; Eli Chapman
Journal:  FASEB J       Date:  2022-03       Impact factor: 5.191

5.  Temperature Regulates Stability, Ligand Binding (Mg2+ and ATP), and Stoichiometry of GroEL-GroES Complexes.

Authors:  Thomas E Walker; Mehdi Shirzadeh; He Mirabel Sun; Jacob W McCabe; Andrew Roth; Zahra Moghadamchargari; David E Clemmer; Arthur Laganowsky; Hays Rye; David H Russell
Journal:  J Am Chem Soc       Date:  2022-02-02       Impact factor: 15.419

6.  Characterization of group II chaperonins from an acidothermophilic archaeon Picrophilus torridus.

Authors:  Yohei Y Yamamoto; Kanako Tsuchida; Keiichi Noguchi; Naoki Ogawa; Hiroshi Sekiguchi; Yuji C Sasaki; Masafumi Yohda
Journal:  FEBS Open Bio       Date:  2016-06-14       Impact factor: 2.693

Review 7.  Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins.

Authors:  Ryo Iizuka; Takashi Funatsu
Journal:  Biophys Physicobiol       Date:  2016-04-22

Review 8.  Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle.

Authors:  Celeste Weiss; Fady Jebara; Shahar Nisemblat; Abdussalam Azem
Journal:  Front Mol Biosci       Date:  2016-12-08

9.  HSP60 possesses a GTPase activity and mediates protein folding with HSP10.

Authors:  Tomoya Okamoto; Hiroshi Yamamoto; Ikuru Kudo; Kazuya Matsumoto; Masafumi Odaka; Ewa Grave; Hideaki Itoh
Journal:  Sci Rep       Date:  2017-12-05       Impact factor: 4.379

10.  Folding of maltose binding protein outside of and in GroEL.

Authors:  Xiang Ye; Leland Mayne; Zhong-Yuan Kan; S Walter Englander
Journal:  Proc Natl Acad Sci U S A       Date:  2018-01-02       Impact factor: 11.205
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.