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The cholesteryl ester transfer protein (CETP) shuttles lipids between lipoproteins. The crystal structure of CETP reveals a lipid-bound tunnel across the protein core, represented here by a tunnel through an underwater aquarium.pp 106-113 | News and Views p 95
An international conference focusing on the Hsp90 molecular chaperone was recently held in Seeon, Germany. The program provided a current synopsis on a wide array of topics, including structural insights, roles in established and novel cellular pathways and disease implications.
A timely study in this issue reports the high-resolution crystal structure of the human plasma protein cholesteryl ester transfer protein (CETP) with its natural lipid ligands. The crystal structure will enhance both basic research on CETP-mediated cholesterol lipid transfer and the design of new drugs that increase plasma high density lipoprotein (HDL) cholesterol.
Histone lysine methylation has a central role in transcriptional regulation and has recently been linked to DNA damage repair. Now it has been shown that the DNA damage repair factor 53BP1 is recruited to DNA double-strand breaks by its tandem tudor domain, which specifically recognizes histone H4 dimethylated at lysine 20.
Selenocysteinyl-tRNASec is used by many organisms from all three domains of life to incorporate selenocysteine (Sec) site-specifically into certain proteins. Two recent reports have identified a new Sec synthase that catalyzes the last step in the generation of this aminoacyl-tRNA in eukarya and archaea.
Eukaryotes transcribe much of their genomes, but little is known about the fidelity of transcriptional initiation by RNA polymerase II in vivo. I suggest that ∼90% of Pol II initiation events in yeast represent transcriptional noise, and that the specificity of initiation is comparable to that of DNA-binding proteins and other biological processes. This emphasizes the need to develop criteria that distinguish transcriptional noise from transcription with a biological function.