Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Many proteins are marked for destruction by covalent attachment of a polyubiquitin chain that directs binding of the modified molecule to the proteasome. A new report demonstrates that an unstructured region of the substrate must also be recognized to begin proteolytic engagement.
Two new studies show that a noncoding RNA, B2, acts as a novel regulator of transcription. This RNA interacts with the general transcription machinery, thereby inhibiting transcription during heat shock response in mice.
EcoR124I is a type I DNA restriction and modification enzyme. The single-molecule magnetic tweezers technique reveals that this sophisticated molecular machine is capable of moving thousands of base pairs of DNA in one binding event.
In a world where nature has designed elegant template-dependent mechanisms for the reproduction of nucleic acid sequences, template-independent RNA polymerases have long been mysterious. Now, two papers provide structural insight into one of these template-independent systems—the addition of the sequence CCA onto the 3′ ends of transfer RNAs.
Cyclic nucleotide phosphodiesterases are widely expressed enzymes that function as critical components of cell signaling pathways. In a new study, key interactions in the catalytic pocket essential for substrate selectivity have been identified for these enzymes, thus introducing novel perspectives for drug design.
