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The Synthesis and Deposition of Storage Proteins: Possible Role of Molecular Chaperones and the Unfolded Protein Response

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Seed Proteins

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Abstract

The notion that proteins are capable of spontaneous folding and assembly is one that enjoyed several decades of support, only being queried with the discovery of a class of proteins which appeared to be involved in assisting polypeptide folding. These observations led to the now well known concept of molecular chaperones, in which proteins undergo assisted folding, usually mediated by a set of ATP-dependent reactions (reviewed in Ellis and van de Reis, 1991). It is also clear that these molecular chaperones are ubiquitous not only to organisms and cell types, but also to different subcellular compartments. The reason for this may be that chaperone proteins are also involved in promoting the translocation of polypeptides (or nascent chains) across the delineating membranes of organelles, such as plastids, mitochondria and the endoplasmic reticulum (ER). In the case of proteins crossing the ER and entering the secretory system, this event is usually a cotranslational process mediated by the signal recognition particle-targeted bound ribosomes which define the rough ER membrane. Within the lumen of the ER are a number of abundant chaperone proteins, the best characterized of these being binding protein (BiP), which was initially characterized on the basis of its interaction with heavy chain immunoglobulins (Haas and Wabl, 1983). Subsequent work in yeast (where the BiP homologue is encoded by the KAR2 gene) and mammalian systems have revealed that BiP is involved in polypeptide translocation and protein folding of a wide range of substrates (reviewed in Gething and Sambrook, 1992).

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Abbreviations

BiP:

binding protein

ER:

endoplasmic reticulum

UPR:

unfolded protein response

UPRE:

unfolded protein response element

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Authors and Affiliations

  1. IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol, BS41 9AF, UK

    Johnathan A. Napier

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  1. Johnathan A. Napier
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Peter R. Shewry Rod Casey

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© 1999 Springer Science+Business Media Dordrecht

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Napier, J.A. (1999). The Synthesis and Deposition of Storage Proteins: Possible Role of Molecular Chaperones and the Unfolded Protein Response. In: Shewry, P.R., Casey, R. (eds) Seed Proteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4431-5_35

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  • DOI: https://doi.org/10.1007/978-94-011-4431-5_35

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-5904-6

  • Online ISBN: 978-94-011-4431-5

  • eBook Packages: Springer Book Archive

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