scholarly journals Hsp90

2001 ◽  
Vol 154 (2) ◽  
pp. 267-274 ◽  
Author(s):  
Jason C. Young ◽  
Ismail Moarefi ◽  
F. Ulrich Hartl
Keyword(s):  
Signal Transduction ◽  
Protein Folding ◽  
Recent Work ◽  
Molecular Chaperones ◽  
Signal Transduction Proteins ◽  
Novel Protein

Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.

Insights into chaperonin function from studies on archaeal thermosomes

2011 ◽  
Vol 39 (1) ◽  
pp. 94-98 ◽  
Author(s):  
Peter Lund
Keyword(s):  
Cell Death ◽  
Protein Folding ◽  
Recent Work ◽  
Mechanism Of Action ◽  
Molecular Chaperones ◽  
Short Review ◽  
Living Cells ◽  
Living Organisms ◽  
Opening And Closing ◽  
Hydrolysis Of

It is now well understood that, although proteins fold spontaneously (in a thermodynamic sense), many nevertheless require the assistance of helpers called molecular chaperones to reach their correct and active folded state in living cells. This is because the pathways of protein folding are full of traps for the unwary: the forces that drive proteins into their folded states can also drive them into insoluble aggregates, and, particularly when cells are stressed, this can lead, without prevention or correction, to cell death. The chaperonins are a family of molecular chaperones, practically ubiquitous in all living organisms, which possess a remarkable structure and mechanism of action. They act as nanoboxes in which proteins can fold, isolated from their environment and from other partners with which they might, with potentially deleterious consequences, interact. The opening and closing of these boxes is timed by the binding and hydrolysis of ATP. The chaperonins which are found in bacteria are extremely well characterized, and, although those found in archaea (also known as thermosomes) and eukaryotes have received less attention, our understanding of these proteins is constantly improving. This short review will summarize what we know about chaperonin function in the cell from studies on the archaeal chaperonins, and show how recent work is improving our understanding of this essential class of molecular chaperones.

The dodo gene family encodes a novel protein involved in signal transduction and protein folding

Gene ◽  
1997 ◽  
Vol 203 (2) ◽  
pp. 89-93 ◽  
Author(s):  
R Maleszka ◽  
A Lupas ◽  
S.D Hanes ◽  
G.L.Gabor Miklos
Keyword(s):  
Signal Transduction ◽  
Protein Folding ◽  
Gene Family ◽  
Novel Protein

scholarly journals Divergence in Coding Sequence and Expression of Different Functional Categories of Immune Genes between Two Wild Rodent Species

2021 ◽  
Vol 13 (3) ◽  
Author(s):  
Xiuqin Zhong ◽  
Max Lundberg ◽  
Lars Råberg
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Immune Function ◽  
Sequence Divergence ◽  
Expression Divergence ◽  
Functional Categories ◽  
Coding Sequence ◽  
Immune Genes ◽  
Genes Encoding ◽  
Signal Transduction Proteins

Abstract Differences in immune function between species could be a result of interspecific divergence in coding sequence and/or expression of immune genes. Here, we investigate how the degree of divergence in coding sequence and expression differs between functional categories of immune genes, and if differences between categories occur independently of other factors (expression level, pleiotropy). To this end, we compared spleen transcriptomes of wild-caught yellow-necked mice and bank voles. Immune genes expressed in the spleen were divided into four categories depending on the function of the encoded protein: pattern recognition receptors (PRR); signal transduction proteins; transcription factors; and cyto- and chemokines and their receptors. Genes encoding PRR and cyto-/chemokines had higher sequence divergence than genes encoding signal transduction proteins and transcription factors, even when controlling for potentially confounding factors. Genes encoding PRR also had higher expression divergence than genes encoding signal transduction proteins and transcription factors. There was a positive correlation between expression divergence and coding sequence divergence, in particular for PRR genes. We propose that this is a result of that divergence in PRR coding sequence leads to divergence in PRR expression through positive feedback of PRR ligand binding on PRR expression. When controlling for sequence divergence, expression divergence of PRR genes did not differ from other categories. Taken together, the results indicate that coding sequence divergence of PRR genes is a major cause of differences in immune function between species.

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits

1998 ◽  
Vol 12 (6) ◽  
pp. 469-478 ◽  
Author(s):  
Michael Seeger ◽  
Regine Kraft ◽  
Katherine Ferrell ◽  
Dawadschargal Bech‐Otschir ◽  
Renate Dumdey ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Complex ◽  
26S Proteasome ◽  
Proteasome Subunits ◽  
Novel Protein

scholarly journals Teasing Apart the Role of the Ribosome and Molecular Chaperones in Cellular Protein Folding

2018 ◽  
Vol 114 (3) ◽  
pp. 414a
Author(s):  
Rayna M. Addabbo ◽  
Matthew D. Dalphin ◽  
Yue Liu ◽  
Miranda F. Mecha ◽  
Silvia Cavagnero
Keyword(s):  
Protein Folding ◽  
Molecular Chaperones ◽  
Cellular Protein

scholarly journals Drug Screening on Signal Transduction Proteins Via μ-Patterned Surfaces

2012 ◽  
Vol 102 (3) ◽  
pp. 31a
Author(s):  
Peter Lanzerstorfer ◽  
Stefan Sunzenauer ◽  
Mario Brameshuber ◽  
Gerhard J. Schütz ◽  
Shin-Ichiro Takahashi ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Drug Screening ◽  
Patterned Surfaces ◽  
Signal Transduction Proteins
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