Publications by authors named "M J Churcher"
Article Synopsis
- The SBDS protein and GTPase EFL1 work together to prepare 60S ribosomal subunits for translation by removing the antiassociation factor eIF6, although the exact process was not previously understood.
- Researchers used cryo-electron microscopy (cryo-EM) to illustrate how human SBDS and EFL1 interact with ribosomal subunits, helping to reveal key structural details.
- The study showed that SBDS plays a critical role in ensuring the ribosome's functional integrity, and that the mechanism of eIF6 release can be disrupted in certain forms of leukemia.
The recessive disorder poikiloderma with neutropenia (PN) is caused by mutations in the C16orf57 gene that encodes the highly conserved USB1 protein. Here, we present the 1.1 Å resolution crystal structure of human USB1, defining it as a member of the LigT-like superfamily of 2H phosphoesterases.
View Article and Find Full Text PDFThe contribution of histone-DNA interactions to nucleosome positioning in vivo is currently a matter of debate. We argue here that certain nucleosome positions, often in promoter regions, in yeast may be, at least in part, specified by the DNA sequence. In contrast other positions may be poorly specified.
View Article and Find Full Text PDF