IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v464y2010i7287d10.1038_nature08817.html
   My bibliography  Save this article

Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome

Author

Listed:
  • Heinz Neumann

    (Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

  • Kaihang Wang

    (Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

  • Lloyd Davis

    (Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

  • Maria Garcia-Alai

    (Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

  • Jason W. Chin

    (Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

Abstract

Protein-designing ribosomes Although chemists can devise novel amino acids with desirable properties, only a few of these amino acids have been successfully introduced into proteins by the cellular machinery. Even then, it is possible to add only one unnatural amino acid to a protein at a time. In theory the use of quadruplet codons, rather than the triplets used in natural protein synthesis, provides added flexibility in the form of extra blank codons available for assignment to unusual amino acids. Natural ribosomes are very inefficient at decoding quadruplets, and cannot be evolved to do it better as they would then misread the entire proteome. Jason Chin and colleagues get around this problem by creating and synthetically evolving parallel or 'orthogonal' ribosomes that efficiently decode quadruple codons using unnatural tRNA synthase/tRNA pairs. This system has the potential to allow the incorporation of up to 200 novel amino acids in genetically encoded designer proteins.

Suggested Citation

  • Heinz Neumann & Kaihang Wang & Lloyd Davis & Maria Garcia-Alai & Jason W. Chin, 2010. "Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome," Nature, Nature, vol. 464(7287), pages 441-444, March.
  • Handle: RePEc:nat:nature:v:464:y:2010:i:7287:d:10.1038_nature08817
    DOI: 10.1038/nature08817
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature08817
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature08817?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Molly F. Parsons & Matthew F. Allan & Shanshan Li & Tyson R. Shepherd & Sakul Ratanalert & Kaiming Zhang & Krista M. Pullen & Wah Chiu & Silvi Rouskin & Mark Bathe, 2023. "3D RNA-scaffolded wireframe origami," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Jairus Rossi, 2013. "The Socionatural Engineering of Reductionist Metaphors: A Political Ecology of Synthetic Biology," Environment and Planning A, , vol. 45(5), pages 1127-1143, May.
    3. Diogo Bessa-Neto & Gerti Beliu & Alexander Kuhlemann & Valeria Pecoraro & Sören Doose & Natacha Retailleau & Nicolas Chevrier & David Perrais & Markus Sauer & Daniel Choquet, 2021. "Bioorthogonal labeling of transmembrane proteins with non-canonical amino acids unveils masked epitopes in live neurons," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    4. Clinton A. L. McFeely & Bipasana Shakya & Chelsea A. Makovsky & Aidan K. Haney & T. Ashton Cropp & Matthew C. T. Hartman, 2023. "Extensive breaking of genetic code degeneracy with non-canonical amino acids," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    5. Luke J. Dowman & Sameer S. Kulkarni & Juan V. Alegre-Requena & Andrew M. Giltrap & Alexander R. Norman & Ashish Sharma & Liliana C. Gallegos & Angus S. Mackay & Adarshi P. Welegedara & Emma E. Watson , 2022. "Site-selective photocatalytic functionalization of peptides and proteins at selenocysteine," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. Yong Wang & Jingming Zhang & Boyang Han & Linzhi Tan & Wenkang Cai & Yuxuan Li & Yeyu Su & Yutong Yu & Xin Wang & Xiaojiang Duan & Haoyu Wang & Xiaomeng Shi & Jing Wang & Xing Yang & Tao Liu, 2023. "Noncanonical amino acids as doubly bio-orthogonal handles for one-pot preparation of protein multiconjugates," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:464:y:2010:i:7287:d:10.1038_nature08817. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.