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    Unravelling Ribosome function through structural studies

    Javed, A. and Orlova, Elena (2020) Unravelling Ribosome function through structural studies. In: Harris, J.R. and Marles-Wright, J. (eds.) Macromolecular Protein Complexes II: Structure and Function. Subcellular Biochemistry 93. Springer. ISBN 9783030281502. (In Press)

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    Abstract

    Ribosomes are biological nanomachine that synthesise all proteins within a cell. It took decades to reveal the architecture of this essential cellular component. The understanding the structure-function relationship of this nanomachine needed the utilisisation of different biochemical, biophysical and structural techniques. Structural studies combined with mutagenesis of the different ribosomal complexes comprising various RNAs and proteins enabled us to understand how this machine works inside a cell. Nowadays quite a number of ribosomal structures were published that confirmed biochemical studies on particular steps of protein synthesis by the ribosome. At the present moment four major steps were identified: initiation, elongation, termination and recycling. These steps lead us to the important question how the ribosome function can be regulated. Advances in technology for cryo electron microscopy: sample preparations, image recording, developments in algorithms for image analysis and processing significantly helped in revelation of structural details of the ribosome. We now have a library of ribosome structures from prokaryotes to eukaryotes that enable us to understand the complex mechanics of this nanomachine. As this structural library continues to grow, we gradually improve our understanding of this process and how it can be regulated and how the specific ribosomes can be stalled or activated, or completely disabled. This review provides a comprehensive overview of ribosomal structures that represent structural snapshots of the ribosome at its different functional states. Better understanding rises more particular questions that have to be addressed by determination structures of more complexes.

    Metadata

    Item Type: Book Section
    Additional Information: Series ISSN: 0306-0225
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 07 Oct 2019 09:28
    Last Modified: 10 Oct 2019 04:22
    URI: http://eprints.bbk.ac.uk/id/eprint/29335

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