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.
Work from de la Mata and Kornblihtt suggests that the C-terminal domain (CTD) of RNA polymerase II recruits the splicing repressor SRp20, thus influencing alternative splicing. Since the CTD is an elongated and flexible structure tagged by phosphate groups, the snake-like and flagged creature depicted in "Drago" by Xul Solar here represents this domain, and its interactive nature. Foundation Pan Klub-Museo Xul Solar reserved rights. pp 973-980, News and Views p 952
Recent additions to the helicase family include motor proteins that do not actually unwind DNA, but rather translocate it. By sensing short polar sequences that orient the bacterial chromosome, the FtsK helicase translocates DNA so as to align the termini of replicated chromosomes with each other, facilitating the late stages of chromosome segregation.
Crystal structures of T4 RNA ligase 2 trapped at different stages of a multistep reaction show how one enzyme active site juggles three phosphoryl transfer reactions to join two RNA strands. The structures also show how the ligase enzyme selectively recognizes the sugar pucker of ribose to achieve catalytic specificity toward RNA-containing substrates.
Recent data suggest that the C-terminal domain of RNA polymerase II can repress exon inclusion via a mechanism not explained by the prevailing models for cotranscriptional splicing regulation.
The DEAD-box ATPase Ded1 unwinds duplex RNA with a single-stranded overhang; however, Ded1 requires the overhang not for translocation but rather for loading onto the duplex. This surprising finding expands the mechanistic repertoire for the ubiquitous DExD/H-box family.