Article
Multidisciplinary Sciences
Kimberly Jia Yi Low, Anandalakshmi Venkatraman, Jodhbir S. Mehta, Konstantin Pervushin
Summary: Protein aggregation and deposition in the form of amyloid fibrils is a characteristic feature of amyloid diseases. While most research focuses on inhibiting amyloid formation, it is equally important to understand the disaggregation mechanisms and their potential therapeutic applications. This review compiles the known mechanisms of amyloid disaggregation and explores the use of disaggregases for treating amyloidosis.
JOURNAL OF ADVANCED RESEARCH
(2022)
Article
Biochemistry & Molecular Biology
Haneul Yoo, Jared A. M. Bard, Evgeny Pilipenko, D. Allan Drummond
Summary: Recent research has shown that heat-induced protein aggregates are actually evolved adaptive biomolecular condensates, with chaperone activity contributing to their regulation, rather than toxic misfolding as previously thought. The yeast disaggregation system can rapidly disperse heat-induced biomolecular condensates, differing in molecular requirements and mechanistic behavior from heat-induced aggregate dispersal. This work highlights the need to expand the proteotoxic interpretation of the heat shock response to include adaptive, chaperone-mediated regulation.
Article
Biochemistry & Molecular Biology
Erika V. Grosfeld, Anastasia Yu. Beizer, Alexander A. Dergalev, Michael O. Agaphonov, Alexander I. Alexandrov
Summary: Protein misfolding is a common feature of aging, various diseases, and stresses. Recent research has shown that misfolded proteins can be gathered into specific compartments, which can limit their harmful effects. Chaperones play a crucial role in the formation of these misfolded protein deposits and can also be used to mark them.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Digvijay Singh, Prajna Tripathi, Rahul Sharma, Sonam Grover, Janendra K. Batra
Summary: The N-terminal domain of Mtb ClpB plays a crucial role in the interaction with its co-partners and in the prevention of aggregation of proteins. The substrate binding pocket identified in this study, comprising of nine amino acid residues forming an alpha-helix, is important for the function of ClpB in repairing and resolubilizing aggregated proteins.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
(2023)
Article
Multidisciplinary Sciences
Arpit Gupta, Alfred M. Lentzsch, Alex Siegel, Zanlin Yu, Un Seng Chio, Yifan Cheng, Shu-ou Shan
Summary: Ring-forming AAA(+) chaperones like Skd3 act as both disaggregases and protein refolding enzymes, and their assembly states play a crucial role in determining their activities. High-resolution structures of Skd3 hexamers capture the ratchet-like motions that mediate substrate extraction, while further assembly into dodecameric cages allows solubilized substrate proteins to attain near-native states. Mutants defective in dodecamer assembly retain disaggregase activity but are impaired in client refolding, highlighting the importance of the hexameric and dodecameric states in Skd3's functions.
Review
Environmental Sciences
Jieting Wu, Tian Gao, Jianing Hu, Lei Zhao, Chang Yu, Fang Ma
Summary: Plants respond to stresses by expressing sHSPs, which play significant roles in inhibiting protein aggregation, protecting cell integrity, and improving resistance. This review systematically summarizes the classification, structure, and functions of sHSPs in plants, with a focus on their roles in promoting fruit ripening and plant growth, protecting photosynthesis, and improving antioxidant activity. The production and regulatory mechanisms of sHSPs are also discussed, along with recent efforts to constitutively express sHSPs in transgenic plants to enhance stress resistance.
SCIENCE OF THE TOTAL ENVIRONMENT
(2022)
Article
Multidisciplinary Sciences
Alexis Tomaszewski, Rebecca Wang, Eduardo Sandoval, Jin Zhu, Jian Liu, Rong Li
Summary: Accumulation of protein aggregates is a hallmark of cellular aging and degenerative disorders. This study reveals that protein aggregates formed under stress can transition from a solid to a liquid state upon stress attenuation, accompanied by a reduction in aggregate number.
Article
Biochemistry & Molecular Biology
Christopher Sun, Leah Slade, Prisca Mbonu, Hunter Ordner, Connor Mitchell, Matthew Mitchell, Fu-Cheng Liang
Summary: This study investigates the effect of a novel protein chaperone, cpSRP43, on Aβ aggregation. The results show that cpSRP43 can effectively prevent and reverse Aβ aggregation, keeping Aβ in the soluble monomeric form. This research may provide new insights for the treatment of Alzheimer's disease.
Article
Biochemical Research Methods
Xiaojing Sui, Dezerae Cox, Shuai Nie, Gavin E. Reid, Danny M. Hatters
Summary: During the recovery from heat shock, eukaryotic cells rapidly down-regulate prefoldins and translation machinery, while mobilizing protein quality control mechanisms, changing cellular energy metabolism, translational activity, and actin cytoskeleton. Long-term adaptation to stress involves the renewal of core cellular components.
JOURNAL OF PROTEOME RESEARCH
(2022)
Review
Biochemistry & Molecular Biology
Axel Leppert, Helen Poska, Michael Landreh, Axel Abelein, Gefei Chen, Jan Johansson
Summary: The BRICHOS protein superfamily is associated with various human diseases and can modulate the aggregation pathways of amyloid-forming substrates. The ability to interfere with different aggregation pathways depends on the quaternary structure and surface motifs of BRICHOS domains. This review provides an overview of the BRICHOS protein family and discusses the diverse molecular chaperone-like functions of BRICHOS domains, as well as the potential use of the BRICHOS domain as a treatment for protein aggregation disorders with blood-brain barrier permeability.
Article
Biochemistry & Molecular Biology
Anna Harari, Guy Zoltsman, Tal Levin, Rina Rosenzweig
Summary: This study structurally characterizes the interaction between Hsp104 NTD and substrates by using NMR spectroscopy. The NTD has a substrate-binding groove that specifically recognizes exposed hydrophobic stretches in Hsp104 substrates. The NTD itself also has chaperoning activities to protect the substrates from further misfolding and aggregation.
Article
Biochemistry & Molecular Biology
Hongtao Li, Liqing Hu, Crist William Cuffee, Mahetab Mohamed, Qianbin Li, Qingdai Liu, Lei Zhou, Qinglian Liu
Summary: Hsp110s are a unique class of molecular chaperones essential for maintaining protein homeostasis. They have strong chaperone activity preventing protein aggregation and serve as the major nucleotide-exchange factor for Hsp70 chaperones. Hsp110s contain nucleotide-binding and substrate-binding domains, with ATP binding being crucial for their function and leading to close contacts between these domains.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Witold Jaworek, Marc Sylvester, Giovanna Cenini, Wolfgang Voos
Summary: Hsp78 is a mitochondrial chaperone that interacts with a wide variety of proteins related to metabolic functions and plays a role in stress-induced protein aggregation and disaggregation.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Article
Multidisciplinary Sciences
Anwar Sadat, Satyam Tiwari, S. Sunidhi, Aseem Chaphalkar, Manisha Kochar, Mudassar Ali, Zainab Zaidi, Akanksha Sharma, Kanika Verma, Kannan Boosi Narayana Rao, Manjul Tripathi, Asmita Ghosh, Deepika Gautam, Atul, Arjun Ray, Koyeli Mapa, Kausik Chakraborty
Summary: The surface charge properties of the GroEL/ES chaperonin cavity, especially the negative charges, play a crucial role in its ability to assist protein folding. However, the negative-charge density varies significantly among different bacterial species and is lowest in eukaryotic GroEL/ES homologs. The chaperoning mechanism of GroEL may have changed during evolution to accommodate different mutations on their substrates.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Biochemistry & Molecular Biology
Nina Kurokawa, Rio Midorikawa, Manami Nakamura, Keiichi Noguchi, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Masafumi Yohda
Summary: The study examined the oligomeric structural change of CgHspB1 using sedimentation velocity analytical ultracentrifugation. It was found that at low temperatures, CgHspB1 exists as an 18-mer and is relatively unstable, partially dissociating into smaller oligomers. At elevated temperatures, the 24-mer is more stable and in dynamic equilibrium with the dissociated oligomers in the hexameric unit. Additionally, the disulfide bond between conserved cysteine residues plays a role in stabilizing the hexamers.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Cell Biology
Naveen Kumar Chandappa Gowda, Jayasankar Mohanakrishnan Kaimal, Anna E. Masser, Wenjing Kang, Marc R. Friedlander, Claes Andreasson
MOLECULAR BIOLOGY OF THE CELL
(2016)
Article
Biochemistry & Molecular Biology
Anna E. Masser, Ganapathi Kandasamy, Jayasankar Mohanakrishnan Kaimal, Claes Andreasson
Article
Cell Biology
Ganapathi Kandasamy, Claes Andreasson
JOURNAL OF CELL SCIENCE
(2018)
Article
Biochemistry & Molecular Biology
Naveen K. C. Gowda, Jayasankar M. Kaimal, Roman Kityk, Chammiran Daniel, Jobst Liebau, Marie Ohman, Matthias P. Mayer, Claes Andreasson
NATURE STRUCTURAL & MOLECULAR BIOLOGY
(2018)
Article
Biochemistry & Molecular Biology
Naveen K. C. Gowda, Jayasankar M. Kaimal, Roman Kityk, Chammiran Daniel, Jobst Liebau, Marie Ohman, Matthias P. Mayer, Claes Andreasson
NATURE STRUCTURAL & MOLECULAR BIOLOGY
(2018)
Article
Cell Biology
Deike J. Omnus, Thorsten Pfirrmann, Claes Andreasson, Per O. Ljungdahl
MOLECULAR BIOLOGY OF THE CELL
(2011)
Article
Multidisciplinary Sciences
Thorsten Pfirrmann, Ashwin Lokapally, Claes Andreasson, Per Ljungdahl, Thomas Hollemann
Article
Multidisciplinary Sciences
Claes Andreasson, Anna J. Schick, Susanne M. Pfeiffer, Mihail Sarov, Francis Stewart, Wolfgang Wurst, Joel A. Schick
Article
Multidisciplinary Sciences
Naveen Kumar Chandappa Gowda, Ganapathi Kandasamy, Marceli S. Froehlich, R. Juergen Dohmen, Claes Andreasson
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2013)
Article
Biochemical Research Methods
Mats A. Holmberg, Naveen Kumar Chandappa Gowda, Claes Andreasson
PROTEIN EXPRESSION AND PURIFICATION
(2014)
Review
Biochemistry & Molecular Biology
Claes Andreasson, Martin Ott, Sabrina Buettner
Article
Biology
Anna E. Masser, Wenjing Kang, Joydeep Roy, Jayasankar Mohanakrishnan Kaimal, Jany Quintana-Cordero, Marc R. Friedlander, Claes Andreasson
Article
Genetics & Heredity
Sarah K. Gersing, Yong Wang, Martin Gronbaek-Thygesen, Caroline Kampmeyer, Lene Clausen, Martin Willemoes, Claes Andreasson, Amelie Stein, Kresten Lindorff-Larsen, Rasmus Hartmann-Petersen
Summary: Canavan disease is a severe neurodegenerative disorder genetically linked to the ASPA gene. The ASPA C152W variant undergoes increased proteasomal degradation due to interference with the de novo folding pathway, although its native structure is largely preserved. Quality control components like Hsp70 and Hsp110 play key roles in the degradation of ASPA C152W, suggesting potential therapeutic targets for protein misfolding diseases.