The Chaperonin Folding Machine
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Review Article Functional Subunits of Eukaryotic Chaperonin CCT/Tric in Protein Folding
SAGE-Hindawi Access to Research Journal of Amino Acids Volume 2011, Article ID 843206, 16 pages doi:10.4061/2011/843206 Review Article Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding M. Anaul Kabir,1 Wasim Uddin,1 Aswathy Narayanan,1 Praveen Kumar Reddy,1 M. Aman Jairajpuri,2 Fred Sherman,3 and Zulfiqar Ahmad4 1 Molecular Genetics Laboratory, School of Biotechnology, National Institute of Technology Calicut, Kerala 673601, India 2 Department of Biosciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India 3 Department of Biochemistry and Biophysics, University of Rochester Medical Center, NY 14642, USA 4 Department of Biology, Alabama A&M University, Normal, AL 35762, USA Correspondence should be addressed to M. Anaul Kabir, [email protected] Received 15 February 2011; Accepted 5 April 2011 Academic Editor: Shandar Ahmad Copyright © 2011 M. Anaul Kabir et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Molecular chaperones are a class of proteins responsible for proper folding of a large number of polypeptides in both prokaryotic and eukaryotic cells. Newly synthesized polypeptides are prone to nonspecific interactions, and many of them make toxic aggregates in absence of chaperones. The eukaryotic chaperonin CCT is a large, multisubunit, cylindrical structure having two identical rings stacked back to back. Each ring is composed of eight different but similar subunits and each subunit has three distinct domains. CCT assists folding of actin, tubulin, and numerous other cellular proteins in an ATP-dependent manner. -
"Hsp70 Chaperones"
Hsp70 Chaperones Advanced article Elizabeth A Craig, University of Wisconsin, Madison, Wisconsin, USA Article Contents . Introduction Jaroslaw Marszalek, University of Gdansk, Gdansk, Poland . Hsp70:Client Protein Interaction Cycle . Proliferation of Hsp70 and J-protein Genes . Function and Evolution of Mitochondrial Hsp70 Systems . Conclusions: Versatility of Hsp70 System Allows for Adaptation to New Functions Online posting date: 15th March 2011 Via their interaction with client proteins, Hsp70 molecu- stress. In some cases they also facilitate transfer of client lar chaperone machines function in a variety of cellular proteins to proteolytic systems, particularly when refolding processes, including protein folding, translocation of into the native state is unachievable. See also: Chaperones, proteins across membranes and assembly/disassembly of Chaperonin and Heat-Shock Proteins The ability of Hsp70 chaperones to be involved in such protein complexes. Such machines are composed of a core diverse cellular functions, whereas relying on a single bio- Hsp70, as well as a J-protein and a nucleotide exchange chemical activity, an adenosine triphosphate (ATP)- factor as co-chaperones. These co-factors regulate the dependent client binding and release cycle, is remarkable. cycle of adenosine triphosphate (ATP) hydrolysis and Here, to illustrate the molecular mechanisms and evo- nucleotide exchange, which is critical for Hsp70’s inter- lutionary history behind the specialisation of Hsp70 sys- action with client proteins. Cellular compartments often tems we focus on mitochondrial Hsp70 systems, as they contain multiple Hsp70s, J-proteins and nucleotide exemplify two major strategies of Hsp70 specialisation: exchange factors. The capabilities of Hsp70s to carry out (i) amplification and diversification of HSP70 genes and diverse cellular functions can result from either special- (ii) multiplication and specialisation of genes encoding isation of an Hsp70 or by interaction of a multifunctional their J-proteins co-chaperones (Figure 1). -
Chaperonin Function: Folding by Forced Unfolding
R EPORTS (1985); N. Romani et al., ibid. 169, 1169 (1989); C. migrated was measured with the clonotypic antibody 26. J. G. Cyster, J. Exp. Med. 189, 447 (1999). Heufler et al., ibid. 176, 1221 (1992). to TCR KJ1-26 (28). Overnight incubation of day 2 27. G. G. MacPherson, C. D. Jenkins, M. J. Stein, C. Ed- 23. R. Bonecchi et al., ibid. 187, 129 (1998). draining lymph node cells (at 107 cells/ml) in medium wards, J. Immunol. 154, 1317 (1995). 24. Anti-OVA (DO11.10) T cell receptor (TCR) transgenic containing interleukin-2 (IL-2) (4 ng/ml) increased 28. K. Haskins et al., J. Exp. Med. 157, 1149 (1983). 1 lymph node cells (5 3 106 cells) were transferred to the sensitivity of activated KJ1-26 cells to MDC 29. We thank R. Locksley, S. Luther, K. Reif, and A. Weiss for comments on the manuscript; M. Ansel for help BALB/c mice that were immunized 1 day later with (14). Therefore, IL-2–cultured cells were used in ex- with the in vivo transfer experiments; and C. 100-mg OVA in Freund’s complete adjuvant (25). periments to detect chemokine production by puri- McArthur for cell sorting. Supported in part by NIH fied lymph node DCs and stromal cells. Draining (pool of brachial, axillary, and inguinal) and grant AI-40098, the Pew Foundation (J.G.C.), and the nondraining (mesenteric) lymph node cells were iso- 25. E. R. Kearney, K. A. Pape, D. Y. Loh, M. K. Jenkins, American Lung Association (H.L.T.). lated 1 to 5 days later and used in MDC chemotaxis Immunity 1, 327 (1994); K. -
Chaperonin-Assisted Protein Folding: a Chronologue
Quarterly Reviews of Chaperonin-assisted protein folding: Biophysics a chronologue cambridge.org/qrb Arthur L. Horwich1,2 and Wayne A. Fenton2 1Howard Hughes Medical Institute, Yale School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, CT 06510, USA and 2Department of Genetics, Yale School of Medicine, Boyer Center, 295 Congress Avenue, New Invited Review Haven, CT 06510, USA Cite this article: Horwich AL, Fenton WA (2020). Chaperonin-assisted protein folding: a Abstract chronologue. Quarterly Reviews of Biophysics This chronologue seeks to document the discovery and development of an understanding of – 53, e4, 1 127. https://doi.org/10.1017/ oligomeric ring protein assemblies known as chaperonins that assist protein folding in the cell. S0033583519000143 It provides detail regarding genetic, physiologic, biochemical, and biophysical studies of these Received: 16 August 2019 ATP-utilizing machines from both in vivo and in vitro observations. The chronologue is orga- Revised: 21 November 2019 nized into various topics of physiology and mechanism, for each of which a chronologic order Accepted: 26 November 2019 is generally followed. The text is liberally illustrated to provide firsthand inspection of the key Key words: pieces of experimental data that propelled this field. Because of the length and depth of this Chaperonin; GroEL; GroES; Hsp60; protein piece, the use of the outline as a guide for selected reading is encouraged, but it should also be folding of help in pursuing the text in direct order. Author for correspondence: Arthur L. Horwich, E-mail: [email protected] Table of contents I. Foundational discovery of Anfinsen and coworkers – the amino acid sequence of a polypeptide contains all of the information required for folding to the native state 7 II. -
Structure-Function Relationship and Their Role in Protein Folding
Chapter 8 1 Molecular Chaperones: Structure-Function 2 Relationship and their Role in Protein Folding 3 Bhaskar K. Chatterjee, Sarita Puri, Ashima Sharma, Ashutosh Pastor, 4 and Tapan K. Chaudhuri 5 Abstract During heat shock conditions a plethora of proteins are found to play a 6 role in maintaining cellular homeostasis. They play diverse roles from folding of 7 non-native proteins to the proteasomal degradation of harmful aggregates. A few 8 out of these heat shock proteins (Hsp) help in the folding of non-native substrate 9 proteins and are termed as molecular chaperones. Various structural and functional 10 adaptations make them work efficiently under both normal and stress conditions. 11 These adaptations involve transitions to oligomeric structures, thermal stability, 12 efficient binding affinity for substrates and co-chaperones, elevated synthesis during 13 shock conditions, switching between ‘holding’ and ‘folding’ functions etc. Their 14 ability to function under various kinds of stress conditions like heat shock, cancers, 15 neurodegenerative diseases, and in burdened cells due to recombinant protein pro- 16 duction makes them therapeutically and industrially important biomolecules. 17 Keywords Chaperone assisted folding · Heat shock · Molecular chaperones · 18 Protein folding · Structure-function of chaperones 19 Abbreviations 20 ACD α-crystallin domain 21 ADP Adenosine di-phosphate 22 ATP Adenosine tri-phosphate 23 CCT Chaperonin containing TCP-1 24 CIRCE Controlling inverted repeat of chaperone expression 25 Bhaskar K. Chatterjee, Sarita Puri, Ashima Sharma, and Ashutosh Pastor authors are equally contributed. B. K. Chatterjee · S. Puri · A. Sharma · A. Pastor · T. K. Chaudhuri (*) Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, HauzKhas, New Delhi, India e-mail: [email protected] © Springer International Publishing AG 2018 181 A. -
Structure, Hormonal Regulation and Chromosomal Location of Genes Encoding Barley (1-+A)-B-Xylan Endohydrolases
l;),, (!. s,9 47 STRUCTURE, HORMONAL RB,GULA CHROMOSOMAL LOCATION OF GENES ENCODING BARLEY (1+4)- p-XYLAI\ ENDOHYDROLASES by MITALI BANIK, B.Sc. (Hons.), M.Sc. A thesis submitted in fulfillment of the requirement for the degree of Doctor of Philosophy Department of Plant Science, Division of Agricultural and Natural Resource Sciences, TheUniversity of Adelaide, Waite Campus, Glen Osmond,5064 Australia October, 1996 1l STATEMENT OF AUTHORSHIP Except where reference is made in the text of the thesis, this thesis contains no material published elsewhere or extracted in whole or in part from a thesis presented by me for another degree or diploma. No other person's work has been used without due acknowledgment in the main text of the thesis. This thesis has not been submitted for the award of any other degree or diploma in any other tertiary institution. MITALI BANIK October, 1996 o lll ACKNOWLBDGMENTS I would like to express my deepest sense of gratitude and indebtedness to my supervisor, Professor Geoffrey B. Fincher, Head of Department, Plant Science, University of Adelaide for his constant guidance, infinite patience, encouragement and invaluable suggestions throughout my studies. I wish to express my immense gratitude to Professor Derek Bewley, Department of Botany, University of Guelph, Canada for his constructive criticism during the preparation of this thesis. I am also grateful to Drs. Frank Gubler and John V. Jacobsen, CSIRO Division of Plant Industry, Canberra for providing a cDNA library. I wish to thank Dr. Simon Robinson, Senior Scientist, CSIRO for his constructive suggestions throughout the duration of my research project. -
Role of CCT Chaperonin in the Disassembly of Mitotic Checkpoint Complexes
Role of CCT chaperonin in the disassembly of mitotic checkpoint complexes Sharon Kaisaria, Danielle Sitry-Shevaha, Shirly Miniowitz-Shemtova, Adar Teichnera, and Avram Hershkoa,1 aUnit of Biochemistry, Rappaport Faculty of Medicine, Technion-Israel Institute of Technology, Haifa 31096, Israel Contributed by Avram Hershko, December 14, 2016 (sent for review November 23, 2016; reviewed by Michele Pagano and Alexander Varshavsky) The mitotic checkpoint system prevents premature separation of thebindingoftheATPasetoMCC(13,14).TheenergyofATP sister chromatids in mitosis and thus ensures the fidelity of hydrolysis is apparently used in this process to promote a confor- chromosome segregation. When this checkpoint is active, a mitotic mational change of Mad2 back from C-Mad2 to O-Mad2, leading checkpoint complex (MCC), composed of the checkpoint proteins to loss of its affinity for Cdc20 in MCC and thus to Mad2 release. Mad2, BubR1, Bub3, and Cdc20, is assembled. MCC inhibits the By the action of TRIP13 and p31comet, MCC is converted to a ubiquitin ligase anaphase promoting complex/cyclosome (APC/C), remnant, called BC-1, in which Cdc20 is still associated with whose action is necessary for anaphase initiation. When the check- BubR1 (15). Cdc20 is released from BubR1 in MCC by a dif- point signal is turned off, MCC is disassembled, a process required ferent process involving the phosphorylation of Cdc20 by Cdk1 for exit from checkpoint-arrested state. Different moieties of MCC (16). We noticed, however, that a considerable part of the release are disassembled by different ATP-requiring processes. Previous of Cdc20 from MCC was due to a phosphorylation-independent, work showed that Mad2 is released from MCC by the joint action comet but ATP-dependent process (16). -
Chaperonin 10 from Escherichia Coli (C7438)
Chaperonin 10 from Escherichia coli recombinant, expressed in E. coli overproducing strain Product Number C7438 Storage Temperature 2–8 C Synonym: GroES The folding activity of a 1:1 molar mixture of GroEL and GroES is determined using urea-denatured rhodanese. Product Description At least a 2-fold increase in reactivation of rhodanese is The chaperonin proteins GroES (Chaperonin 10) and observed compared to spontaneous reactivation. GroEL (Chaperonin 60) are heat shock proteins that assist the folding of nascent and heat-destabilized The inhibition of the ATPase activity of GroEL by GroES proteins.1 GroES (Chaperonin 10) is a complex of at a molar ratio of 2:1 (GroES:GroEL) is determined to 6-8 units of a 10 kDa monomer, with a multimer be 40-60%. molecular mass of 60-80 kDa. Aggregation studies on chaperonin 10 monomer from different species have Purity: 95% (SDS-PAGE) been reported.2 GroEL (Chaperonin 60) is a tetradecamer of a 58 kDa monomer, with a multimer Precautions and Disclaimer molecular mass of 800 kDa. For R&D use only. Not for drug, household, or other uses. Please consult the Safety Data Sheet for GroEL and GroES can be used to stabilized labile information regarding hazards and safe handling proteins and reactivate denatured proteins. Refolding practices. and reactivation of denatured enzymes such as the photosynthetic enzyme RuBisCO,3 mitochondrial Preparation Instructions rhodanese,4 and glutamine synthase5 have been The product is soluble in water (0.5 mg/mL). reported. Storage/Stability Folding of proteins by these chaperonins requires It is recommended to store the product desiccated at GroEL, Mg-ATP (GroEL has ATPase activity), and in 2–8 C. -
Technische Universität München
TECHNISCHE UNIVERSITÄT MÜNCHEN Department Chemie Lehrstuhl für Biotechnologie Analysis of small heat shock proteins and their interaction with substrate proteins Marina Angelika Kreuzeder Vollständiger Abdruck der von der Fakultät für Chemie der Technischen Universität München zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften (Dr. rer. nat.) genehmigten Dissertation. Vorsitzender: Prof. Dr. Bernd Reif Prüfer der Dissertation 1. Prof. Dr. Johannes Buchner 2. Prof. Dr. Michael Sattler Die Dissertation wurde am 18.09.2017 bei der Technischen Universität München eingereicht und durch die Fakultät für Chemie am 02.11.2017 angenommen. Für meine Eltern Contents Contents 1. INTRODUCTION.............................................................................................. 1 1.1 Protein folding .................................................................................................................................. 1 1.2 Cell stress and heat shock proteins ........................................................................................... 3 1.3 Molecular chaperones .................................................................................................................... 5 1.4 ATP- dependent chaperones ........................................................................................................ 6 1.5 Small heat shock proteins ............................................................................................................. 9 1.5.1 Structure of Hsps ..................................................................................................................................... -
Chaperonins: Nanocarriers with Biotechnological Applications
nanomaterials Review Chaperonins: Nanocarriers with Biotechnological Applications Sergio Pipaón 1 , Marcos Gragera 1 , M. Teresa Bueno-Carrasco 1, Juan García-Bernalt Diego 1 , Miguel Cantero 1, Jorge Cuéllar 1 , María Rosario Fernández-Fernández 1 and José María Valpuesta 1,2,* 1 Centro Nacional de Biotecnología (CNB-CSIC). Darwin, 3. 28049 Madrid, Spain; [email protected] (S.P.); [email protected] (M.G.); [email protected] (M.T.B.-C.); [email protected] (J.G.-B.D.); [email protected] (M.C.); [email protected] (J.C.); [email protected] (M.R.F.-F.) 2 Unidad Asociada de Nanobiotecnología (IMDEA Nanociencia), 28049 Madrid, Spain * Correspondence: [email protected] Abstract: Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins. Chaperonins are found in two main conformations, one in which the cavity is open and ready to recognise and trap unfolded client proteins, and a “closed” form in which folding takes place. The conspicuous properties of this structure (a cylinder containing a cavity that allows confinement) and the potential to control its closure and aperture have inspired a number of nanotechnological applications that will be described in this review. Keywords: molecular chaperones; chaperonins; nanocarriers; nanoreactors Citation: Pipaón, S.; Gragera, M.; Bueno-Carrasco, M.T.; García-Bernalt 1. Chaperonins: Structure and Function Diego, J.; Cantero, M.; Cuéllar, J.; In the crowded environment of the cell, most proteins need assistance to acquire their Fernández-Fernández, M.R.; Valpuesta, J.M. -
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US 2006.0068405A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2006/0068405 A1 Diber et al. (43) Pub. Date: Mar. 30, 2006 (54) METHODS AND SYSTEMIS FOR Correspondence Address: ANNOTATING BOMOLECULAR Martin D. Moynihan SEQUENCES PRTSI, Inc. (76) Inventors: Alex Diber, Rishon-LeZion (IL); Sarah P.O. Box 16446 Pollock, Tel-Aviv (IL); Zurit Levine, Arlington, VA 22215 (US) Herzlia (IL); Sergey Nemzer, RaAnana (IL); Vladimir Grebinskiy, Highland Park, NJ (US); Brian Meloon, (21) Appl. No.: 11/043,860 Plainsboro, NJ (US); Andrew Olson, Northport, NY (US): Avi Rosenberg, Kfar Saba (IL); Ami Haviv, (22) Filed: Jan. 27, 2005 Hod-HaSharon (IL); Shaul Zevin, Mevaseret Zion (IL); Tomer Zekharia, Givataim (IL); Zipi Shaked, Tel-Aviv (IL); Moshe Olshansky, Haifa (IL); Related U.S. Application Data Ariel Farkash, Haifa (IL); Eyal Privman, Tel-Aviv (IL); Amit Novik, (60) Provisional application No. 60/539,129, filed on Jan. Beit-YeHoshua (IL); Naomi Keren, 27, 2004. Givat Shmuel (IL); Gad S. Cojocaru, Ramat-HaSharon (IL); Pinch as Akiva, Publication Classification Ramat-Gan (IL); Yossi Cohen, Surrey (GB); Ronen Shemesh, Modi In (IL); (51) Int. C. Osnat Sella-Tavor, Kfar-Kish (IL); CI2O I/68 (2006.01) Liat Mintz, East brunswick, NJ (US); G06F 9/00 (2006.01) Hanging Xie, Lambertville, NJ (US); Dvir Dahary, Tel-Aviv (IL); Erez (52) U.S. Cl. ................................................... 435/6; 702/20 Levanon, Petach-Tikva (IL); Shiri Freilich, Haifa (IL); Nili Beck, Kfar Saba (IL); Wei-Yong Zhu, Plainsboro, (57) ABSTRACT NJ (US); Alon Wasserman, New York, NY (US); Chen Chermesh, Mishmar HaShiva (IL); Idit Azar, Tel-Aviv (IL); Polypeptide sequences and polynucleotide sequences are Rotem Sorek, Rechovot (IL); Jeanne provided.