The chaperone-like activity of α-crystallin is considered to play an important role in the maintenance of the transparency of the eye lens. However, in the case of aging and in diabetes, the chaperone function of α-crystallin is compromized, resulting in cataract formation. Several post-translational modifications, including non-enzymatic glycation, have been shown to affect the chaperone funct...

A fundamental role of the Hsp90-Cdc37 chaperone system in mediating maturation of protein kinase clients and supporting kinase functional activity is essential for the integrity and viability of signaling pathways involved in cell cycle control and organism development. Despite significant advances in understanding structure and function of molecular chaperones, the molecular mechanisms and gui...

JCB • VOLUME 167 • NUMBER 2 • 2004 190 A chaperone feels the heat chaperone is supposed to keep its cool when temperatures get hot. But Syed Rizvi, Laura Mancino, Malini Raghavan (University of Michigan, Ann Arbor, MI), and colleagues show that calreticulin—a glycoprotein chaperone—starts to melt in the heat. The resulting structural changes actually improve its chaperone activity and may also ...

JCB • VOLUME 167 • NUMBER 2 • 2004 190 A chaperone feels the heat chaperone is supposed to keep its cool when temperatures get hot. But Syed Rizvi, Laura Mancino, Malini Raghavan (University of Michigan, Ann Arbor, MI), and colleagues show that calreticulin—a glycoprotein chaperone—starts to melt in the heat. The resulting structural changes actually improve its chaperone activity and may also ...

La proteins are conserved factors in eukaryotes that bind and protect the 3' trailers of pre-tRNAs from exonuclease digestion via sequence-specific recognition of UUU-3'OH. La has also been hypothesized to assist pre-tRNAs in attaining their native fold through RNA chaperone activity. In addition to binding polymerase III transcripts, human La has also been shown to enhance the translation of s...

Cytosolic eukaryotic 2-Cys-peroxiredoxins have been widely reported to act as dual-function proteins, either detoxifying reactive oxygen species or acting as chaperones to prevent protein aggregation. Several stimuli, including peroxide-mediated sulfinic acid formation at the active site cysteine, have been proposed to trigger the chaperone activity. However, the mechanism underlying this activ...

PURPOSE The G98R mutation in αA-crystallin is associated with autosomal dominant cataract in humans. We have reported that mutant G98R protein has substrate-dependent chaperone activity. Further studies on this G98R mutant protein revealed that mutant protein shows reduced oligomeric stability and accelerated subunit dissociation at a low protein concentration. The purpose of present study was ...

BACKGROUND Significant portion of alphaA-crystallin in human lenses exists as C-terminal residues cleaved at residues 172, 168, and 162. Chaperone activity, determined with alcohol dehydrogenase (ADH) and betaL-crystallin as target proteins, was increased in alphaA(1-172) and decreased in alphaA(1-168) and alphaA(1-162). The purpose of this study was to show whether the absence of the C-termina...

Safeguarding the proteome is central to the health of the cell. In multi-cellular organisms, the composition of the proteome, and by extension, protein-folding requirements, varies between cells. In agreement, chaperone network composition differs between tissues. Here, we ask how chaperone expression is regulated in a cell type-specific manner and whether cellular differentiation affects chape...

Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. ...