Article
Biochemistry & Molecular Biology
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
Summary: This study outlines the structural similarities and functional differences between ESKAPE GroES/GroEL and Escherichia coli GroES/GroEL, and reveals the importance of allosteric compatibility between these two proteins for cell viability. Interestingly, differences in allosteric compatibility do not necessarily result in differences in refolding rates.
Article
Chemistry, Physical
Nicolas Macro, Long Chen, Yushan Yang, Tridib Mondal, Lijuan Wang, Amnon Horovitz, Dongping Zhong
Summary: The research findings suggest that the GroEL cavity provides a unique water environment that may facilitate the folding of substrate proteins.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2021)
Article
Food Science & Technology
Abraham Rivera-Ramirez, Rosalba Salgado-Morales, Janette Onofre-Lemus, Blanca I. Garcia-Gomez, Humberto Lanz-Mendoza, Edgar Dantan-Gonzalez
Summary: This study evaluates the chaperonin and insecticidal activities of different GroEL proteins, and highlights the high insecticidal activity and phenoloxidase system activation of GroELXn protein. Furthermore, GroEL proteins can enhance the toxic activity of the ExoA toxin, possibly through their chaperonin activity.
Article
Multidisciplinary Sciences
Sofia S. Kudryavtseva, Evgeny B. Pichkur, Igor A. Yaroshevich, Aleksandra A. Mamchur, Irina S. Panina, Andrei V. Moiseenko, Olga S. Sokolova, Vladimir I. Muronetz, Tatiana B. Stanishneva-Konovalova
Summary: In this study, cryo-EM was used to resolve two nucleotide-bound structures of the bullet-shaped GroEL-GroES complex, revealing different orientations of their apical domains. The results suggest that the bound nucleotides correspond to ADP and appear at low ATP:ADP ratios.
SCIENTIFIC REPORTS
(2021)
Review
Biochemistry & Molecular Biology
Maria S. Yurkova, Alexey N. Fedorov
Summary: Chaperones play a vital role in cell life and can be used in biotechnology and scientific research.
Article
Microbiology
Jared Sivinski, Andrew J. Ambrose, Iliya Panfilenko, Christopher J. Zerio, Jason M. Machulis, Niloufar Mollasalehi, Lynn K. Kaneko, Mckayla Stevens, Anne-Marie Ray, Yangshin Park, Chunxiang Wu, Quyen Q. Hoang, Steven M. Johnson, Eli Chapman
Summary: The GroES/GroEL chaperonin system in bacteria is essential and potentially a target for antibiotics. However, the functional differences between GroES/GroEL chaperonins from different bacteria, including ESKAPE pathogens, suggest potential challenges in developing chaperonin-targeted antibiotics.
Article
Multidisciplinary Sciences
Yanyan Zhao, Michael F. Schmid, Judith Frydman, Wah Chiu
Summary: The researchers used cryo-EM to analyze chaperonins and found negative cooperativity in ATP binding and random distribution of nucleotides within the structure.
NATURE COMMUNICATIONS
(2021)
Article
Biology
Caixuan Liu, Mingliang Jin, Shutian Wang, Wenyu Han, Qiaoyu Zhao, Yifan Wang, Cong Xu, Lei Diao, Yue Yin, Chao Peng, Lan Bao, Yanxing Wang, Yao Cong
Summary: This study reveals the conformational landscape of TRiC-mediated tubulin folding along TRiC's ATPase cycle and the interaction sites between tubulin and the closed TRiC chamber using cryo-EM and XL-MS analyses.
COMMUNICATIONS BIOLOGY
(2023)
Article
Chemistry, Multidisciplinary
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
Summary: The study used variable-temperature electrospray ionization native mass spectrometry to analyze the stability of GroEL and GroEL-GroES complexes, revealing destabilization at lower temperatures and the formation of previously unreported reaction products. Additionally, it was found that temperature, Mg2+, and ATP concentrations influence the stoichiometry of the GroEL-GroES complex.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2022)
Article
Multidisciplinary Sciences
David P. Klebl, Matthew C. Feasey, Emma L. Hesketh, Neil A. Ranson, Heiko Wurdak, Frank Sobott, Robin S. Bon, Stephen P. Muench
Summary: The structure of HSPD1 in the apo state was determined using cryo-EM, revealing its mostly single ring assemblies without co-chaperonin. Compared to GroEL, HSPD1 shows a rotation and increased flexibility of the apical domain. This new insight into the structural changes during the catalytic cycle of HSPD1 may lead to new treatments targeting HSPD1 against various diseases, including glioblastoma.
Article
Biotechnology & Applied Microbiology
Prasanth Karaiyan, Catherine Ching Han Chang, Eng-Seng Chan, Beng Ti Tey, Ramakrishnan Nagasundara Ramanan, Chien Wei Ooi
Summary: Sequence-based screening is widely used in discovering novel microbial enzymes, but lacks experimental characterization. This study presents a systematic screening method to identify soluble and functional proteins using in silico techniques. The success rate of producing soluble and active DmoA enzyme is 71%, and interestingly, the soluble form of DmoA exhibits oxidoreductase activity. DmoA from Janthinobacterium sp. AD80 shows the highest NADH oxidation activity.
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Tatsuya Niwa, Yuhei Chadani, Hideki Taguchi
Summary: The Lon protease has been identified as the major protease involved in the degradation of obligate GroE substrates in GroE-depleted cells. Deletion of other major E. coli chaperones does not significantly affect the folding of these substrates, indicating that their folding is primarily dependent on GroE.
Article
Microbiology
Kristen Schroeder, Kristina Heinrich, Ines Neuwirth, Kristina Jonas
Summary: This study reveals the functional interaction between GroESL and the bacterial cell division machinery, with GroESL not only affecting peptidoglycan biosynthesis during cell division, but also influencing the dynamics of divisome assembly.
Review
Biochemistry & Molecular Biology
Hideki Taguchi, Ayumi Koike-Takeshita
Summary: Protein folding can be hindered by protein aggregation, but this can be prevented by chaperones in the cell. The bacterial chaperonin GroEL forms complexes with its cochaperonin GroES to facilitate protein folding. Recent studies have identified numerous GroE-dependent clients, shedding light on the role of chaperonins in protein folding and evolution.
FRONTIERS IN MOLECULAR BIOSCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Karla N. Valenzuela-Valderas, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduno
Summary: Research has shown that the bacterial pathogen Legionella pneumophila's chaperonin protein HtpB has a unique function in interaction with the eukaryotic protein ECM29, which can be mapped to specific amino acid positions.