NDLI: Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome

Content Provider	PubMed Central
Author	Forster, Anthony C.
Copyright Year	2009
Abstract	Aminoacyl-transfer RNAs contain four standardized units: amino acids, an invariant 3′-terminal CCA, trinucleotide anticodons and tRNA bodies. The degree of interchangeability of the three variable modules is poorly understood, despite its role in evolution and the engineering of translation to incorporate unnatural amino acids. Here, a purified translation system is used to investigate effects of various module swaps on the efficiency of multiple ribosomal incorporations of unnatural aminoacyl-tRNA substrates per peptide product. The yields of products containing three to five adjacent l-amino acids with unnatural side chains are low and cannot be improved by optimization or explained simply by any single factor tested. Though combinations of modules that allow quantitative single unnatural incorporations are found readily, finding combinations that enable efficient synthesis of products containing multiple unnatural amino acids is challenging. This implies that assaying multiple, as opposed to single, incorporations per product is a more stringent assay of substrate activity. The unpredictability of most results illustrates the multifactorial nature of substrate recognition and the value of synthetic biology for testing our understanding of translation. Data indicate that the degree of interchangeability of the modules of aminoacyl-tRNAs is low.
Related Links	http://dx.doi.org/10.1093/nar/gkp240
Ending Page	3755
Page Count	9
Starting Page	3747
File Format	PDF
ISSN	03051048
e-ISSN	13624962
Journal	Nucleic Acids Research
Issue Number	11
Volume Number	37
Language	English
Publisher	Oxford University Press
Publisher Date	2009-06-01
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Genetics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics

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Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome

Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome

Archaeal aminoacyl-tRNA synthetases interact with the ribosome to recycle tRNAs

Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates

Ribosome-associated protein that inhibits translation at the aminoacyl-tRNA binding stage

Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

Pulling the ribosome out of frame by +1 at a programmed frameshift site by cognate binding of aminoacyl-tRNA.

Archaeal aminoacyl-tRNA synthetases interact with the ribosome to recycle tRNAs

Erratum: Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome

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Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome

Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome

Archaeal aminoacyl-tRNA synthetases interact with the ribosome to recycle tRNAs

Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates

Ribosome-associated protein that inhibits translation at the aminoacyl-tRNA binding stage

Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

Pulling the ribosome out of frame by +1 at a programmed frameshift site by cognate binding of aminoacyl-tRNA.

Archaeal aminoacyl-tRNA synthetases interact with the ribosome to recycle tRNAs

Erratum: Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome