Ontology highlight
ABSTRACT:
SUBMITTER: Mangeol P
PROVIDER: S-EPMC3215066 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Mangeol Pierre P Bizebard Thierry T Chiaruttini Claude C Dreyfus Marc M Springer Mathias M Bockelmann Ulrich U
Proceedings of the National Academy of Sciences of the United States of America 20111024 45
Ribosomal (r-) RNA adopts a well-defined structure within the ribosome, but the role of r-proteins in stabilizing this structure is poorly understood. To address this issue, we use optical tweezers to unfold RNA fragments in the presence or absence of r-proteins. Here, we focus on Escherichia coli r-protein L20, whose globular C-terminal domain (L20C) recognizes an irregular stem in domain II of 23S rRNA. L20C also binds its own mRNA and represses its translation; binding occurs at two different ...[more]