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1-28 of 28
Keywords: chaperone
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Articles
Deciphering the mechanism and function of Hsp100 unfoldases from protein structure
Available to Purchase
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2022) 50 (6): 1725–1736.
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...
Articles
Stress-induced O-GlcNAcylation: an adaptive process of injured cells
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2017) 45 (1): 237–249.
Published: 15 February 2017
..., microRNA-423-5p was demonstrated to target the 3′-untranslated region (3′-UTR) of OGT mRNA, suppressing OGT expression [ 30 ]. chaperone glycoprotein heat shock response mgea5 OGT signal transduction Cells and tissues respond to environmental and physiological injury by reprogramming...
Articles
Periplasmic quality control in biogenesis of outer membrane proteins
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2015) 43 (2): 133–138.
Published: 07 April 2015
... 8 2014 © The Authors Journal compilation © 2015 Biochemical Society 2015 outer membrane protein periplasm protease chaperone single molecule detection FRET The cell envelope of Gram-negative bacteria consists of the inner membrane (IM), the outer membrane (OM...
Articles
About the dangers, costs and benefits of living an aerobic lifestyle
Available to PurchaseDaniela Knoefler, Lars I.O. Leichert, Maike Thamsen, Claudia M. Cremers, Dana Reichmann, Michael J. Gray, Wei-Yun Wholey, Ursula Jakob
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2014) 42 (4): 917–921.
Published: 11 August 2014
... of different proteins against stress-induced protein aggregation. We have demonstrated that polyP has protein chaperone-like properties, binding to unfolding proteins with high affinity and releasing them to other ATP-dependent chaperones once non-stress conditions are restored and polyP is re-converted...
Articles
Chaperone-mediated autophagy: dedicated saviour and unfortunate victim in the neurodegeneration arena
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2013) 41 (6): 1483–1488.
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...
Articles
Knotting pathways in proteins
Available to PurchaseJoanna I. Sułkowska, Jeffrey K. Noel, César A. Ramírez-Sarmiento, Eric J. Rawdon, Kenneth C. Millett, José N. Onuchic
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2013) 41 (2): 523–527.
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...
Articles
Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?
Available to PurchaseThierry 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
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2012) 40 (6): 1522–1527.
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...
Articles
Evolutionary selection for protein aggregation
Available to PurchaseNatalia Sanchez de Groot, Marc Torrent, Anna Villar-Piqué, Benjamin Lang, Salvador Ventura, Jörg Gsponer, M. Madan Babu
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2012) 40 (5): 1032–1037.
Published: 19 September 2012
... be addressed to either of these authors (email [email protected] or [email protected] ). 10 7 2012 © The Authors Journal compilation © 2012 Biochemical Society 2012 amyloid chaperone evolution protein aggregation A large number of proteins have been found...
Articles
Diverse functional manifestations of intrinsic structural disorder in molecular chaperones
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2012) 40 (5): 963–968.
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...
Articles
Histone transfer among chaperones
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2012) 40 (2): 357–363.
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...
Articles
The yeast prion protein Ure2: insights into the mechanism of amyloid formation
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2011) 39 (5): 1359–1364.
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...
Articles
Targeting proteins to the plant nuclear envelope
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2010) 38 (3): 733–740.
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...
Articles
Assembly manual for the proteasome regulatory particle: the first draft
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2010) 38 (1): 6–13.
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...
Articles
Chaperone-assisted assembly of the proteasome core particle
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2010) 38 (1): 29–33.
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...
Articles
Chaperones and protein folding in the archaea
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2009) 37 (1): 46–51.
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...
Articles
Iron–sulfur cluster biosynthesis
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2008) 36 (6): 1112–1119.
Published: 19 November 2008
... in the assembly, storage or transfer of Fe–S clusters. chaperone cysteine desulfurase glutaredoxin iron–sulfur cluster scaffold Clusters involving iron and inorganic sulfide that are attached to the polypeptide primarily via cysteinate iron ligation constitute one of the most ubiquitous...
Articles
Cellular factors important for the de novo formation of yeast prions
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2008) 36 (5): 1083–1087.
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...
Articles
Chaperone-driven proteasome assembly
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2008) 36 (5): 807–812.
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...
Articles
Role(s) of Cdc48/p97 in mitosis
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2008) 36 (1): 126–130.
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...
Articles
Common and specific mechanisms of AAA+ proteins involved in protein quality control
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2008) 36 (1): 120–125.
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...
Articles
From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins
Available to PurchaseTeru Ogura, Yuka Matsushita-Ishiodori, Ai Johjima, Masayo Nishizono, Shingo Nishikori, Masatoshi Esaki, Kunitoshi Yamanaka
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2008) 36 (1): 68–71.
Published: 22 January 2008
... Genes Dev. 2004 18 369 374 9 Schlieker C. Weibezahn J. Patzelt H. Tessarz P. Strub C. Zeth K. Erbse A. Schneider-Mergener J. Chin J.W. Schultz P.G. Bukau B. Mogk A. Substrate recognition by the AAA+ chaperone ClpB Nat. Struct. Mol. Biol...
Articles
Protein import into mitochondria
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2005) 33 (5): 1019–1023.
Published: 26 October 2005
... and to the unravelling of the mechanisms of preprotein translocation. 1 To whom correspondence should be addressed (email [email protected] ). 21 6 2005 © 2005 The Biochemical Society 2005 chaperone import motor mitochondria mitochondrial translocase protein translocation TIM23...
Articles
Covalent cofactor attachment to proteins: cytochrome c biogenesis
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2005) 33 (4): 792–795.
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...
Articles
‘Nature-inspired’ drug–protein complexes as inhibitors of Aβ aggregation
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2005) 33 (4): 543–547.
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...
Articles
Lsm proteins and RNA processing
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2005) 33 (3): 433–438.
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...
Articles
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2004) 32 (4): 626–628.
Published: 01 August 2004
... 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 of interferon-γ was seen on re-stimulation...
Articles
Mechanism of substrate recognition by Hsp70 chaperones
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2004) 32 (4): 617–621.
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...
Articles
The chaperonins: perspectives from the Archaea
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Journal:
Biochemical Society Transactions
Biochem Soc Trans (2003) 31 (3): 681–685.
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...
