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Articles

Deciphering the mechanism and function of Hsp100 unfoldases from protein structure

Grace Lee, Rebecca S. Kim, Sang Bum Lee, Sukyeong Lee, Francis T.F. Tsai

Biochem Soc Trans (2022) 50 (6): 1725–1736.

DOI: https://doi.org/10.1042/BST20220590

Published: 01 December 2022

...Grace Lee; Rebecca S. Kim; Sang Bum Lee; Sukyeong Lee; Francis T.F. Tsai Hsp100 chaperones, also known as Clp proteins, constitute a family of ring-forming ATPases that differ in 3D structure and cellular function from other stress-inducible molecular chaperones. While the vast majority of ATP...

View article titled, Deciphering the mechanism and function of Hsp100 unfoldases from protein structure

Articles

Stress-induced O-GlcNAcylation: an adaptive process of injured cells

Marissa R. Martinez, Thiago Braido Dias, Peter S. Natov, Natasha E. Zachara

Biochem Soc Trans (2017) 45 (1): 237–249.

DOI: https://doi.org/10.1042/BST20160153

Published: 15 February 2017

... Society 2017 chaperone glycoprotein heat shock response mgea5 OGT signal transduction Cells and tissues respond to environmental and physiological injury by reprogramming transcription, translation, metabolism, and signal transduction to affect repair and survival, and if necessary...

View article titled, Stress-induced O-GlcNAcylation: an adaptive process of injured cells

Articles

Periplasmic quality control in biogenesis of outer membrane proteins

Zhi Xin Lyu, Xin Sheng Zhao

Biochem Soc Trans (2015) 43 (2): 133–138.

DOI: https://doi.org/10.1042/BST20140217

Published: 07 April 2015

... 8 2014 © The Authors Journal compilation © 2015 Biochemical Society 2015 outer membrane protein periplasm protease chaperone single molecule detection FRET Each subunit of DegP contains a trypsin-like protease domain and two PDZ domains, which have been shown...

View article titled, Periplasmic quality control in biogenesis of outer membrane proteins

Articles

About the dangers, costs and benefits of living an aerobic lifestyle

Daniela Knoefler, Lars I.O. Leichert, Maike Thamsen, Claudia M. Cremers, Dana Reichmann, Michael J. Gray, Wei-Yun Wholey, Ursula Jakob

Biochem Soc Trans (2014) 42 (4): 917–921.

DOI: https://doi.org/10.1042/BST20140108

Published: 11 August 2014

... To whom correspondence should be addressed (email ujakob@umich.edu ). 25 4 2014 © The Authors Journal compilation © 2014 Biochemical Society 2014 aging chaperone host defence oxidative stress protein unfolding Living an aerobic lifestyle is treacherous. ROS (reactive oxygen...

View article titled, About the dangers, costs and benefits of living an aerobic lifestyle

Articles

Chaperone-mediated autophagy: dedicated saviour and unfortunate victim in the neurodegeneration arena

Jaime L. Schneider, Ana Maria Cuervo

Biochem Soc Trans (2013) 41 (6): 1483–1488.

DOI: https://doi.org/10.1042/BST20130126

Published: 20 November 2013

...Jaime L. Schneider; Ana Maria Cuervo The importance of cellular quality-control systems in the maintenance of neuronal homoeostasis and in the defence against neurodegeneration is well recognized. Chaperones and proteolytic systems, the main components of these cellular surveillance mechanisms...

View article titled, Chaperone-mediated autophagy: dedicated saviour and unfortunate victim in the neurodegeneration arena

Articles

Knotting pathways in proteins

Joanna I. Sułkowska, Jeffrey K. Noel, César A. Ramírez-Sarmiento, Eric J. Rawdon, Kenneth C. Millett, José N. Onuchic

Biochem Soc Trans (2013) 41 (2): 523–527.

DOI: https://doi.org/10.1042/BST20120342

Published: 21 March 2013

..., the prevalence of traps in the free energy landscape also increases. Thus, in the case of longer knotted and slipknotted proteins, the folding mechanism is probably supported by chaperones. Overall, results imply that knotted proteins can be folded efficiently and survive evolutionary pressure in order...

View article titled, Knotting pathways in proteins

Articles

Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?

Thierry Touzé, Hélène Barreteau, Meriem El Ghachi, Ahmed Bouhss, Aurélie Barnéoud-Arnoulet, Delphine Patin, Emmanuelle Sacco, Didier Blanot, Michel Arthur, Denis Duché, Roland Lloubès, Dominique Mengin-Lecreulx

Biochem Soc Trans (2012) 40 (6): 1522–1527.

DOI: https://doi.org/10.1042/BST20120189

Published: 21 November 2012

...). ColM cytotoxicity is dependent on FkpA of the targeted cell, a chaperone with peptidylprolyl cis – trans isomerase activity. Dissection of ColM was used to delineate the catalytic domain and to identify the active-site residues. The in vitro activity of the isolated catalytic domain towards lipid II...

View article titled, Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?

Articles

Evolutionary selection for protein aggregation

Natalia Sanchez de Groot, Marc Torrent, Anna Villar-Piqué, Benjamin Lang, Salvador Ventura, Jörg Gsponer, M. Madan Babu

Biochem Soc Trans (2012) 40 (5): 1032–1037.

DOI: https://doi.org/10.1042/BST20120160

Published: 19 September 2012

... be addressed to either of these authors (email nsdgroot@mrc-lmb.cam.ac.uk or madanm@mrc-lmb.cam.ac.uk ). 10 7 2012 © The Authors Journal compilation © 2012 Biochemical Society 2012 amyloid chaperone evolution protein aggregation During evolution, cells have been equipped...

View article titled, Evolutionary selection for protein aggregation

Articles

Diverse functional manifestations of intrinsic structural disorder in molecular chaperones

Denes Kovacs, Peter Tompa

Biochem Soc Trans (2012) 40 (5): 963–968.

DOI: https://doi.org/10.1042/BST20120108

Published: 19 September 2012

...Denes Kovacs; Peter Tompa IDPs (intrinsically disordered proteins) represent a unique class of proteins which show diverse molecular mechanisms in key biological functions. The aim of the present mini-review is to summarize IDP chaperones that have increasingly been studied in the last few years...

View article titled, Diverse functional manifestations of intrinsic structural disorder in molecular chaperones

Articles

Histone transfer among chaperones

Wallace H. Liu, Mair E.A. Churchill

Biochem Soc Trans (2012) 40 (2): 357–363.

DOI: https://doi.org/10.1042/BST20110737

Published: 21 March 2012

... chaperones, which serve multifaceted roles in co-ordinating the interactions of histone proteins with modification enzymes, nucleosome remodellers, other histone chaperones and nucleosomal DNA. The molecular details of the processes by which histone chaperones promote delivery of histones among their many...

View article titled, Histone transfer among chaperones

Articles

The yeast prion protein Ure2: insights into the mechanism of amyloid formation

Li-Jun Chen, Elizabeth B. Sawyer, Sarah Perrett

Biochem Soc Trans (2011) 39 (5): 1359–1364.

DOI: https://doi.org/10.1042/BST0391359

Published: 21 September 2011

... and loses its regulatory function. A number of molecular chaperones have been found to affect the prion properties of Ure2. The studies carried out in our laboratory have been aimed at elucidating the structure of Ure2 fibrils, the mechanism of amyloid formation and the effect of chaperones on the fibril...

View article titled, The yeast prion protein Ure2: insights into the mechanism of amyloid formation

Articles

Targeting proteins to the plant nuclear envelope

Iris Meier, Xiao Zhou, Jelena Brkljacić, Annkatrin Rose, Qiao Zhao, Xianfeng Morgan Xu

Biochem Soc Trans (2010) 38 (3): 733–740.

DOI: https://doi.org/10.1042/BST0380733

Published: 24 May 2010

... transmembrane domain is sufficient for targeting WIP proteins to the nuclear envelope. Nuclear-envelope targeting of WIT proteins requires a coiled-coil domain and is facilitated by HSC70 (heat-shock cognate 70 stress protein) chaperones and a class of plant-specific proteins resembling the RanGAP-targeting...

View article titled, Targeting proteins to the plant nuclear envelope

Articles

Chaperone-assisted assembly of the proteasome core particle

Ana C. Matias, Paula C. Ramos, R. Jürgen Dohmen

Biochem Soc Trans (2010) 38 (1): 29–33.

DOI: https://doi.org/10.1042/BST0380029

Published: 19 January 2010

... chaperones. Assembly of the CP alone involves three conserved proteasome-assembly chaperones [PAC1–PAC2, PAC3–PAC4 and UMP1 (ubiquitin-mediated proteolysis 1)]. Whereas the two heterodimeric PACs have been implicated in the formation of rings of the seven distinct α subunits, UMP1 is important...

View article titled, Chaperone-assisted assembly of the proteasome core particle

Articles

Assembly manual for the proteasome regulatory particle: the first draft

Soyeon Park, Geng Tian, Jeroen Roelofs, Daniel Finley

Biochem Soc Trans (2010) 38 (1): 6–13.

DOI: https://doi.org/10.1042/BST0380006

Published: 19 January 2010

...Soyeon Park; Geng Tian; Jeroen Roelofs; Daniel Finley The proteasome is the most complex protease known, with a molecular mass of approx. 3 MDa and 33 distinct subunits. Recent studies reported the discovery of four chaperones that promote the assembly of a 19-subunit subcomplex of the proteasome...

View article titled, Assembly manual for the proteasome regulatory particle: the first draft

Articles

Chaperones and protein folding in the archaea

Andrew T. Large, Martin D. Goldberg, Peter A. Lund

Biochem Soc Trans (2009) 37 (1): 46–51.

DOI: https://doi.org/10.1042/BST0370046

Published: 20 January 2009

...Andrew T. Large; Martin D. Goldberg; Peter A. Lund A survey of archaeal genomes for the presence of homologues of bacterial and eukaryotic chaperones reveals several interesting features. All archaea contain chaperonins, also known as Hsp60s (where Hsp is heat-shock protein). These are more similar...

View article titled, Chaperones and protein folding in the archaea

Articles

Iron–sulfur cluster biosynthesis

Sibali Bandyopadhyay, Kala Chandramouli, Michael K. Johnson

Biochem Soc Trans (2008) 36 (6): 1112–1119.

DOI: https://doi.org/10.1042/BST0361112

Published: 19 November 2008

... in the assembly, storage or transfer of Fe–S clusters. 19 6 2008 © The Authors Journal compilation © 2008 Biochemical Society 2008 chaperone cysteine desulfurase glutaredoxin iron–sulfur cluster scaffold 1 To whom correspondence should be addressed (email johnson@chem.uga.edu...

View article titled, Iron–sulfur cluster biosynthesis

Articles

Chaperone-driven proteasome assembly

Rina Rosenzweig, Michael H. Glickman

Biochem Soc Trans (2008) 36 (5): 807–812.

DOI: https://doi.org/10.1042/BST0360807

Published: 19 September 2008

... results in a latent 20S core particle that can serve further as a platform for 19S regulatory particle attachment and formation of the biologically active 26S proteasome for ubiquitin-dependent proteolysis. Both general and dedicated proteasome assembly chaperones regulate the efficiency and outcome...

View article titled, Chaperone-driven proteasome assembly

Articles

Cellular factors important for the de novo formation of yeast prions

Mick Tuite, Klement Stojanovski, Frederique Ness, Gloria Merritt, Nadejda Koloteva-Levine

Biochem Soc Trans (2008) 36 (5): 1083–1087.

DOI: https://doi.org/10.1042/BST0361083

Published: 19 September 2008

... acid residues. The molecular mechanism by which the [ PIN + ] prion facilitates de novo [ PSI + ] formation is not fully established, but most probably involves some form of cross-seeding. A number of other cellular factors, in particular chaperones of the Hsp70 (heat-shock protein 70) family...

View article titled, Cellular factors important for the de novo formation of yeast prions

Articles

From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins

Teru Ogura, Yuka Matsushita-Ishiodori, Ai Johjima, Masayo Nishizono, Shingo Nishikori, Masatoshi Esaki, Kunitoshi Yamanaka

Biochem Soc Trans (2008) 36 (1): 68–71.

DOI: https://doi.org/10.1042/BST0360068

Published: 22 January 2008

... be addressed (email ogura@gpo.kumamoto-u.ac.jp ). 28 8 2007 © The Authors Journal compilation © 2008 Biochemical Society 2008 ATPase associated with various cellular activities (AAA) chaperone katanin p97 protease spastin AAA (ATPase associated with various cellular activities...

View article titled, From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins

Articles

Role(s) of Cdc48/p97 in mitosis

Hemmo Meyer, Oliver Popp

Biochem Soc Trans (2008) 36 (1): 126–130.

DOI: https://doi.org/10.1042/BST0360126

Published: 22 January 2008

...Hemmo Meyer; Oliver Popp The ubiquitin-dependent chaperone Cdc48 (cell divison cycle 48)/p97 is involved in a variety of degradative and regulatory processes during interphase that help to maintain cellular homoeostasis. The results available so far suggest that its basic activity is to mobilize...

View article titled, Role(s) of Cdc48/p97 in mitosis

Articles

Common and specific mechanisms of AAA+ proteins involved in protein quality control

Axel Mogk, Tobias Haslberger, Peter Tessarz, Bernd Bukau

Biochem Soc Trans (2008) 36 (1): 120–125.

DOI: https://doi.org/10.1042/BST0360120

Published: 22 January 2008

...Axel Mogk; Tobias Haslberger; Peter Tessarz; Bernd Bukau A protein quality control system, consisting of molecular chaperones and proteases, controls the folding status of proteins and mediates the refolding or degradation of misfolded proteins. Ring-forming AAA+ (ATPase associated with various...

View article titled, Common and specific mechanisms of AAA+ proteins involved in protein quality control

Articles

Protein import into mitochondria

D. Mokranjac, W. Neupert

Biochem Soc Trans (2005) 33 (5): 1019–1023.

DOI: https://doi.org/10.1042/BST0331019

Published: 26 October 2005

... and to the unravelling of the mechanisms of preprotein translocation. 1 To whom correspondence should be addressed (email Neupert@med.uni-muenchen.de ). 21 6 2005 © 2005 The Biochemical Society 2005 chaperone import motor mitochondria mitochondrial translocase protein translocation TIM23...

View article titled, Protein import into mitochondria

Articles

‘Nature-inspired’ drug–protein complexes as inhibitors of Aβ aggregation

M. Bose, J.E. Gestwicki, V. Devasthali, G.R. Crabtree, I.A. Graef

Biochem Soc Trans (2005) 33 (4): 543–547.

DOI: https://doi.org/10.1042/BST0330543

Published: 01 August 2005

... and optimized over millions of years of evolution, we have created a bifunctional molecule [SLF (synthetic ligand for FK506-binding protein)–CR (Congo Red)] that is able to block Aβ (amyloid β) aggregation by borrowing the surface and steric bulk of a cellular chaperone. 1 Present address: Life...

View article titled, ‘Nature-inspired’ drug–protein complexes as inhibitors of Aβ aggregation

Articles

Covalent cofactor attachment to proteins: cytochrome c biogenesis

J.M. Stevens, T. Uchida, O. Daltrop, S.J. Ferguson

Biochem Soc Trans (2005) 33 (4): 792–795.

DOI: https://doi.org/10.1042/BST0330792

Published: 01 August 2005

... that the haem chaperone CcmE ( c ytochrome c m aturation), which is an essential intermediate in the process, also binds haem covalently before transferring the haem to apocytochromes. A single covalent bond is involved and occurs between a haem vinyl group and a histidine residue of CcmE. Several in vitro...

View article titled, Covalent cofactor attachment to proteins: cytochrome c biogenesis

Articles

Lsm proteins and RNA processing

J.D. Beggs

Biochem Soc Trans (2005) 33 (3): 433–438.

DOI: https://doi.org/10.1042/BST0330433

Published: 01 June 2005

... that affect pre-mRNA splicing and degradation, small nucleolar RNA, tRNA processing, rRNA processing and mRNA degradation. These activities suggest RNA chaperone-like roles for Lsm proteins, affecting RNA–RNA and/or RNA–protein interactions. This article reviews the properties of the Sm and Lsm proteins...

View article titled, Lsm proteins and RNA processing

Articles

BCG (Bacille Calmette–Guérin) HspCs (heat-shock protein–peptide complexes) induce T-helper 1 responses and protect against live challenge in a murine aerosol challenge model of pulmonary tuberculosis

C.A.L.S. Colaco, C.R. Bailey, J. Keeble, K.B. Walker

Biochem Soc Trans (2004) 32 (4): 626–628.

DOI: https://doi.org/10.1042/BST0320626

Published: 01 August 2004

... Hsp65 (GroEL) itself. This indicates that the cell-mediated response induced by HspC immunization is directed primarily against the pathogen-derived antigens chaperoned by the Hsp in the HspC preparation, and not the Hsp itself. This contention is supported further by the fact that the maximal induction...

View article titled, BCG (Bacille Calmette–Guérin) HspCs (heat-shock protein–peptide complexes) induce T-helper 1 responses and protect against live challenge in a murine aerosol challenge model of pulmonary tuberculosis

Articles

Mechanism of substrate recognition by Hsp70 chaperones

A. Erbse, M.P. Mayer, B. Bukau

Biochem Soc Trans (2004) 32 (4): 617–621.

DOI: https://doi.org/10.1042/BST0320617

Published: 01 August 2004

...A. Erbse; M.P. Mayer; B. Bukau The role of Hsp70 (heat-shock protein 70) chaperones in assisting protein-folding processes relies on their ability to associate with short peptide stretches of protein substrates in a transient and ATP-controlled manner. In the present study, we review the molecular...

View article titled, Mechanism of substrate recognition by Hsp70 chaperones

Articles

The chaperonins: perspectives from the Archaea

P.A. Lund, A.T. Large, G. Kapatai

Biochem Soc Trans (2003) 31 (3): 681–685.

DOI: https://doi.org/10.1042/bst0310681

Published: 01 June 2003

...P.A. Lund; A.T. Large; G. Kapatai Heat-shock protein (Hsp) 60 chaperones are almost ubiquitous and almost always essential. They can be divided on the basis of sequence homology into two broad types: group I (found in bacteria, mitochondria and chloroplasts) and group II (found in Archaea...

View article titled, The chaperonins: perspectives from the Archaea

NARROW

Deciphering the mechanism and function of Hsp100 unfoldases from protein structure

Stress-induced O-GlcNAcylation: an adaptive process of injured cells

Periplasmic quality control in biogenesis of outer membrane proteins

About the dangers, costs and benefits of living an aerobic lifestyle

Chaperone-mediated autophagy: dedicated saviour and unfortunate victim in the neurodegeneration arena

Knotting pathways in proteins

Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?

Evolutionary selection for protein aggregation

Diverse functional manifestations of intrinsic structural disorder in molecular chaperones

Histone transfer among chaperones

The yeast prion protein Ure2: insights into the mechanism of amyloid formation

Targeting proteins to the plant nuclear envelope

Chaperone-assisted assembly of the proteasome core particle

Assembly manual for the proteasome regulatory particle: the first draft

Chaperones and protein folding in the archaea

Iron–sulfur cluster biosynthesis

Chaperone-driven proteasome assembly

Cellular factors important for the de novo formation of yeast prions

From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins

Role(s) of Cdc48/p97 in mitosis

Common and specific mechanisms of AAA+ proteins involved in protein quality control

Protein import into mitochondria

‘Nature-inspired’ drug–protein complexes as inhibitors of Aβ aggregation

Covalent cofactor attachment to proteins: cytochrome c biogenesis

Lsm proteins and RNA processing

BCG (Bacille Calmette–Guérin) HspCs (heat-shock protein–peptide complexes) induce T-helper 1 responses and protect against live challenge in a murine aerosol challenge model of pulmonary tuberculosis

Mechanism of substrate recognition by Hsp70 chaperones

The chaperonins: perspectives from the Archaea

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