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. 2008 Sep;9(9):822-7.
doi: 10.1038/embor.2008.159.

Synthetic biology: discovering new worlds and new words

Víctor de Lorenzo  1 , Antoine Danchin
Affiliations

Synthetic biology: discovering new worlds and new words

Víctor de Lorenzo et al. EMBO Rep. 2008 Sep.
No abstract available

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Figures

Figure 1
Figure 1
The pillars of synthetic biology. Disciplines in biology, biotechnology, engineering and computing interact to form the foundations of synthetic biology. In addition, research on the origin of life is experiencing a considerable rebirth (Luisi, 2006).
Figure 2
Figure 2
Translation and uridine diphosphate biosynthesis. The gene cluster tsf–pyrH–frr, which encodes the translation elongation factor (EF-T), uridylate kinase (UMK) and the ribosome-recycling factor (RRF), is highly conserved in bacterial genomes. However, translation apparently does not use uridine triphosphate (UTP) in any of its known reactions or its regulation. In bacteria, UMK is found in close association with the bacterial envelope. How and why is this activity related to ribosome recycling? We expect that ribosomes have to recycle in the terminus of the last gene of every operon. This region is generally located downstream from a 3′-region of the messenger RNA that forms a so-called Rho-independent stem and loop structure. These terminators are uracil-rich and must therefore consume a considerable amount of UTP, yielding uridine diphosphate (UDP). One could conjecture that UTP regulates RRF and that the transcription of operons terminates at regions not far from the membrane. 30S and 50S subunits assemble at the 5′ end of the mRNA, which is pulled and translated through the ribosome. At the end of a cistron, the 70S ribosome can immediately begin to translate the next cistron, unless it encounters the formation of a Rho-independent stem and loop structure, which is terminated by a poly(U)-rich tail. The local synthesis of the poly(U) therefore depletes UTP bound to the RRF, which can bind to the 70S ribosome, promoting its dissociation into 30S and 50S subunits.
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