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  • A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy.

A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy.

Nature communications (2017-09-30)
Linda E Franken, Gert T Oostergetel, Tjaard Pijning, Pranav Puri, Valentina Arkhipova, Egbert J Boekema, Bert Poolman, Albert Guskov
要旨

Bacteria downregulate their ribosomal activity through dimerization of 70S ribosomes, yielding inactive 100S complexes. In Escherichia coli, dimerization is mediated by the hibernation promotion factor (HPF) and ribosome modulation factor. Here we report the cryo-electron microscopy study on 100S ribosomes from Lactococcus lactis and a dimerization mechanism involving a single protein: HPF

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酢酸マグネシウム 溶液, BioUltra, for molecular biology, ~1 M in H2O