In Science this week, investigators from the University of California, San Francisco, and the Max Planck Institute report on new proteomic insights into the genome of the human cytomegalovirus. Although the HCMV genome was sequenced two decades ago, its protein-coding potential remains largely undefined. To address this issue, the researchers used ribosome profiling and transcript analysis to “experimentally define the HCMV translation products and follow their temporal expression.” The result was the identification of hundreds of previously unknown open reading frames and the discovery that “regulated use of alternative transcript start sites plays a broad role in enabling tight temporal control of HCMV protein expression and allowing multiple distinct polypeptides to be generated from a single genomic locus.”
Also in Science, Stony Brook University researchers provided a review of the advances made in understanding protein folding since Max Perutz and John Kendrew won the Nobel Prize for determining the structure of a globular protein 50 years ago. They sum up how far investigators have come to answering the three central questions facing the field: What is the physical code by which an amino acid sequence dictates a protein’s native structure; how can proteins fold so fast; and can we devise a computer algorithm to predict protein structures from their sequences? They conclude that while much has been learned, new questions have also arisen, and they stress the often unexpected benefits of untargeted basic science.