منابع مشابه
Protein folding: Chaperones get Hip
In the cell, nascent and completed polypeptides may misfold and aggregate. A class of proteins called molecular chaperones has evolved to facilitate the production of native, functional forms of proteins. These chaperones also aid in the translocation of proteins across biological membranes. The ubiquitous heat-shock protein (Hsp) 70 class of chaperones has been the subject of intensive study o...
متن کاملMolecular chaperones--cellular machines for protein folding.
Proteins are linear polymers synthesized by ribosomes from activated amino acids. The product of this biosynthetic process is a polypeptide chain, which has to adopt the unique three-dimensional structure required for its function in the cell. In 1972, Christian Anfinsen was awarded the Nobel Prize for Chemistry for showing that this folding process is autonomous in that it does not require any...
متن کاملChaperones and protein folding in the archaea.
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 to the type II chaperonins found in the eukaryotic cytosol than to the type I chaperonins found in bacteria, mitochondria and chloroplasts, although...
متن کاملProtein folding: Who chaperones nascent chains in bacteria?
Important advances in biology often occur when problems that have been controversial and seemingly complex are resolved with surprisingly simple and clear answers. Such has been the case with the problem of how proteins fold inside cells, which has seen a number of controversies and solutions in the past decade. A very recent example of this concerns the physiological functions of two molecular...
متن کاملCatalysis of protein folding by chaperones in pathogenic bacteria.
Molecular chaperones are thought to inhibit off-pathway interactions such as aggregation from occurring without influencing the on-pathway formation of native structure. Here, we present a mechanism whereby the family of PapD-like chaperones, which are involved in the formation of adhesive pili in pathogenic bacteria, function by suppressing aggregation while simultaneously catalyzing the foldi...
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ژورنال
عنوان ژورنال: Current Biology
سال: 1996
ISSN: 0960-9822
DOI: 10.1016/s0960-9822(02)00476-1