Hold on to your friends: dedicated chaperones of ribosomal proteins
- Pillet, Benjamin Unit of Biochemistry, Department of Biology, University of Fribourg, Switzerland
- Mitterer, Valentin Institut für Molekulare Biowissenschaften, Universität Graz, Austria
- Kressler, Dieter Unit of Biochemistry, Department of Biology, University of Fribourg, Switzerland
- Pertschy, Brigitte Institut für Molekulare Biowissenschaften, Universität Graz, Austria
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01.01.2017
Published in:
- BioEssays. - 2017, vol. 39, no. 1, p. 1-12
English
Eukaryotic ribosomes are assembled from their components, the ribosomal RNAs and ribosomal proteins, in a tremendously complex, multi-step process, which primarily takes place in the nuclear compartment. Therefore, most ribosomal proteins have to travel from the cytoplasm to their incorporation site on pre-ribosomes within the nucleus. However, due to their particular characteristics, such as a highly basic amino acid composition and the presence of unstructured extensions, ribosomal proteins are especially prone to aggregation and degradation in their unassembled state, hence specific mechanisms must operate to ensure their safe delivery. Recent studies have uncovered a group of proteins, termed dedicated chaperones, specialized in accompanying and guarding individual ribosomal proteins. In this essay, we review how these dedicated chaperones utilize different folds to interact with their ribosomal protein clients and how they ensure their soluble expression and interconnect their intracellular transport with their efficient assembly into pre-ribosomes.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 279081
- DOI 10.1002/bies.201600153
- Persistent URL
- https://folia.unifr.ch/unifr/documents/305274
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