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Faithful chaperones

Szolajska, Ewa and Chroboczek, Jadwiga (2011) Faithful chaperones. Cellular and Molecular Life Sciences, 68 (20). pp. 3307-3322. ISSN 1420-682X

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Official URL: http://dx.doi.org/10.1007/s00018-011-0740-4


This review describes the properties of some rare eukaryotic chaperones that each assist in the folding of only one target protein. In particular, we describe a) the tubulin cofactors, b) p47, which assists in the folding of collagen, c) α-hemoglobin stabilizing protein (AHSP), d) the adenovirus L4-100K protein, which is a chaperone of the major structural viral protein, hexon, and e) HYPK, the huntingtin-interacting protein. These various sized proteins (102 to 1190 amino acids long) are all involved in the folding of oligomeric polypeptides but are otherwise functionally unique, as they each assist only one particular client. This raises a question regarding the biosynthetic cost of the high-level production of such chaperones. As the clients of faithful chaperones are all abundant proteins that are essential cellular or viral components, it is conceivable that this necessary metabolic expenditure withstood evolutionary pressure to minimize biosynthetic costs. Nevertheless, the complexity of the folding pathways in which these chaperones are involved results in error-prone processes. Several human disorders associated with these chaperones are discussed.

Item Type:Article
Uncontrolled Keywords:Tubulin cofactors p47 a-hemoglobin stabilizing protein L4-100 K HYPK
Subjects:Q Science > Q Science (General)
R Medicine > RB Pathology
Divisions:Department of Protein Biosynthesis
ID Code:284
Deposited By: dr Ewa/E Szolajska
Deposited On:29 Nov 2012 15:18
Last Modified:15 Oct 2014 07:59

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