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Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones

Duccio Malinverni, Simone Marsili, Alessandro Barducci, Paolo De Los Rios, Marco Punta
2015 PLoS Computational Biology  
We use the correlated amino acid coevolutions in protein sequences to identify directly interacting amino acids.  ...  Furthermore, we highlight that the features encoding the Hsp70 dimer are more conserved in bacterial than in eukaryotic sequences, suggesting that the known Hsp70/Hsp110 hetero-dimer is a eukaryotic specialization  ...  Acknowledgments We thank Andrea Pagnani, Pierre Goloubinoff, Andrija Finka, Jacques Rougemont and David Fabrice for useful discussions. Author Contributions  ... 
doi:10.1371/journal.pcbi.1004262 pmid:26046683 pmcid:PMC4457872 fatcat:ma77zlfraneixog6xrw5ctppue

The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones

Velasco, Dublang, Moro, Muga
2019 International Journal of Molecular Sciences  
A protein machinery in metazoa, composed of representatives of the Hsp70, Hsp40, and Hsp110 chaperone families, can reactivate protein aggregates.  ...  We revised herein the phosphorylation sites found so far in members of these chaperone families and the functional consequences associated with some of them.  ...  Proteins and domains are drawn on scale according to the length of their amino acid sequences.  ... 
doi:10.3390/ijms20174122 pmid:31450862 pmcid:PMC6747476 fatcat:htsykinvnvh25dvlbalwmjvea4

The Hsp70-Chaperone Machines in Bacteria

Matthias P. Mayer
2021 Frontiers in Molecular Biosciences  
Third, Hsp70s are targeted to their clients by a large number of cochaperones of the J-domain protein (JDP) family and the lifetime of the Hsp70-client complex is regulated by nucleotide exchange factors  ...  In this review I will discuss advances in the understanding of the molecular mechanism of the Hsp70 chaperone machinery focusing mostly on the bacterial Hsp70 DnaK and will compare the two other prokaryotic  ...  Thus, the small and large hydrophobic residues are reversed in the arch of eukaryotic Hsp70s.  ... 
doi:10.3389/fmolb.2021.694012 pmid:34164436 pmcid:PMC8215388 fatcat:hcf6wcjfa5dgnmd4tvw5cqjkqe

The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response

Benjamin J Lang, Martin E Guerrero, Thomas L Prince, Yuka Okusha, Cristina Bonorino, Stuart K Calderwood
2021 Archives of Toxicology  
The effector molecules of the HSR, the Heat Shock Factors (HSFs) and Heat Shock Proteins (HSPs), are also important regulatory targets in the progression of neurodegenerative diseases and cancers.  ...  While named for its vital role in the cellular response to heat stress, various components of the HSR system and the molecular chaperone network execute essential physiological functions as well as responses  ...  Acknowledgements We thank the Department of Radiation Oncology, BIDMC, Harvard Medical School for support and encouragement. Figures 1, 2, 3 , 4, and 6 were created with biorender.com.  ... 
doi:10.1007/s00204-021-03070-8 pmid:34003342 fatcat:n3nwgu2tjjeojbanb5u2qq4gke

Nonspecific Protein Adsorption Requires Large Adhesive Domains on the Surface

Lei Shen, Xiaoyang Zhu
2011 Biophysical Journal  
The success of disorder prediction using a protein's primary structure suggests that the propensity for disorder is encoded in the amino acid sequence.  ...  Previously, we found that net charge per residue segregates IDP sequences along a globule-to-coil transition and speculated that the polymeric characters of an IDP conformational ensemble could be predicted  ... 
doi:10.1016/j.bpj.2010.12.1458 fatcat:yoxdrrrcpnahbkk5j6qn6rb65i

αα-Synuclein Interactions with Hsp70

Elizabeth Middleton, Elizabeth Rhoades
2011 Biophysical Journal  
The success of disorder prediction using a protein's primary structure suggests that the propensity for disorder is encoded in the amino acid sequence.  ...  Previously, we found that net charge per residue segregates IDP sequences along a globule-to-coil transition and speculated that the polymeric characters of an IDP conformational ensemble could be predicted  ... 
doi:10.1016/j.bpj.2010.12.1460 fatcat:ga5zsacko5csvoo5b7jqhzb3wa

Getting a grip on non-native proteins

Peter C Stirling, Victor F Lundin, Michel R Leroux
2003 EMBO Reports  
Here, we explore the nature and occurrence of non-native proteins, and describe the diverse families of molecular chaperones and coordinated cellular responses that have evolved to prevent their misfolding  ...  It is an underappreciated fact that non-native polypeptides are prevalent in the cellular environment.  ...  We acknowledge the Canadian Institutes of Health Research (CIHR) and the National Cancer Institute of Canada for financial support.  ... 
doi:10.1038/sj.embor.embor869 pmid:12776175 pmcid:PMC1319208 fatcat:aw37lj6f7nd63eno3uwssl3syu

Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones

Matthias P. Mayer, Lila M. Gierasch
2018 Journal of Biological Chemistry  
Significant advances in recent years are beginning to unravel the molecular mechanism of this chaperone machine and how they treat their substrate proteins.  ...  Hsp70 chaperones are central hubs of the protein quality control network and collaborate with co-chaperones having a J-domain (an ∼70-residue-long helical hairpin with a flexible loop and a conserved His-Pro-Asp  ...  insertion of an amino acid side chain into the hydrophobic pocket in the SBD␤ and transmits the conformational changes to the NBD (Fig. 3 ) (21) .  ... 
doi:10.1074/jbc.rev118.002810 pmid:30455352 pmcid:PMC6369304 fatcat:ehlivms7urfwdoq5m5emhswoqm

Mechanisms of Protein Folding: Molecular Chaperones and Their Application in Biotechnology

Axel Mogk, Matthias P. Mayer, Elke Deuerling
2002 ChemBioChem  
In 1961 Anfinsen showed that all the information needed for reaching the active 3D structure is encoded in the protein's amino acid sequence.  ...  Introduction Protein folding is the process that leads from the linear amino acid sequence of a polypeptide chain to a defined spatial structure characteristic for the native protein.  ... 
doi:10.1002/1439-7633(20020902)3:9<807::aid-cbic807>3.0.co;2-a pmid:12210979 fatcat:4473nve5ivbi3kq6s2zy73hgjq

Molecular Chaperones ofLeishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes

Jose M. Requena, Ana M. Montalvo, Jorge Fraga
2015 BioMed Research International  
Molecular chaperones are key components in the maintenance of cellular homeostasis and survival, not only during stress but also under optimal growth conditions.  ...  Furthermore, when proteins are damaged, molecular chaperones may also facilitate their refolding or, in the case of irreparable proteins, their removal by the protein degradation machinery of the cell.  ...  Acknowledgments The results and insights presented in this review are the products of the tremendous effort of many researchers working in the field of molecular chaperones and/or Leishmania biology, and  ... 
doi:10.1155/2015/301326 pmid:26167482 pmcid:PMC4488524 fatcat:4egcgkbnezc2fce55jdqbkuhaq

The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders

Federica Scalia, Alessandra Maria Vitale, Radha Santonocito, Everly Conway de Macario, Alberto J. L. Macario, Francesco Cappello
2021 Applied Sciences  
Genetic NCPs are linked to pathogenic variants of chaperone genes encoding, for example, the small Hsp, Hsp10, Hsp40, Hsp60, and CCT-BBS (chaperonin-containing TCP-1- Bardet–Biedl syndrome) chaperones.  ...  Instead, the acquired NCPs are associated with malfunctional chaperones, such as Hsp70, Hsp90, and VCP/p97 with aberrant post-translational modifications.  ...  Conflicts of Interest: The authors declare no conflict of interest.  ... 
doi:10.3390/app11030898 fatcat:expagdxlmnhv7nam3vil3idagm

Intrinsically Disordered Protein Regions Modeled as Isolated Entities Commonly Adopt Ensembles of Collapsed, Globular Conformations

Albert H. Mao, Rohit V. Pappu
2011 Biophysical Journal  
Even though, gp120 from these clades are structurally similar, spatially distant sites may differentially influence conformational motions to modulate the antibody escape in a clade specific manner.  ...  Network analysis indicates that the communities in Cclade gp120 differ the most from B-clade gp120.  ...  The success of disorder prediction using a protein's primary structure suggests that the propensity for disorder is encoded in the amino acid sequence.  ... 
doi:10.1016/j.bpj.2010.12.1461 fatcat:57l6f4qdtrf2ljg4tyrmaqk6xm

Computational Epigenetics: Molecular Dynamics Simulations of the Structure of HP1 Bound to a Variably Modified Histone Tail

George V. Papamokos, George Tziatzos, Anastasia Politou, Demetrios Papageorgiou, Spyros Georgatos, Efthimios Kaxiras
2011 Biophysical Journal  
The success of disorder prediction using a protein's primary structure suggests that the propensity for disorder is encoded in the amino acid sequence.  ...  Previously, we found that net charge per residue segregates IDP sequences along a globule-to-coil transition and speculated that the polymeric characters of an IDP conformational ensemble could be predicted  ... 
doi:10.1016/j.bpj.2010.12.1462 fatcat:lzi6fr7m4vbdtpjdrwy3oqqzxa

Capturing the Initial Autocatalytic Maturation Mechanism of HIV-1 protease at Atomic Resolution

S. Kashif Sadiq, Gianni De Fabritiis
2011 Biophysical Journal  
The success of disorder prediction using a protein's primary structure suggests that the propensity for disorder is encoded in the amino acid sequence.  ...  Previously, we found that net charge per residue segregates IDP sequences along a globule-to-coil transition and speculated that the polymeric characters of an IDP conformational ensemble could be predicted  ... 
doi:10.1016/j.bpj.2010.12.1457 fatcat:ssymrl22wvg53jx76bghpuo7zq

Fast Dynamics of Protein Preservation in Sugar Glasses

David S. Simmons, Marcus T. Cicerone, Jack F. Douglas
2011 Biophysical Journal  
The success of disorder prediction using a protein's primary structure suggests that the propensity for disorder is encoded in the amino acid sequence.  ...  Previously, we found that net charge per residue segregates IDP sequences along a globule-to-coil transition and speculated that the polymeric characters of an IDP conformational ensemble could be predicted  ... 
doi:10.1016/j.bpj.2010.12.1459 fatcat:e5prxjejpvhknju7ckxxdudz34
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