O! She doth teach the torches to burn bright: How JULIET can help authors and repository advocates.

JULIET is a service provided by SHERPA. Its mission is to provide a brief summary of each funding agency’s policy on self-archiving of the published research they have funded. Each entry covers the requirements and details: -Whether archiving is mandatory or encouraged, -What should be deposited -Within what time frame this deposit should take place -Where articles should be deposited -Any conditions attached to this deposit. JULIET interacts with other services such as RoMEO, which listed publisher policies on self-archiving. JULIET is being developed to include funding agency’s policies on open access to data.

The bacterial helicase-primase interaction: a common structural/functional module

The lack of a high-resolution structure for the bacterial helicase-primase complex and the fragmented structural information for the individual proteins have been hindering our detailed understanding of this crucial binary protein interaction. Two new structures for the helicase-interacting domain of the bacterial primases from Escherichia coli and Bacillus stearothermophilus have recently been solved and both revealed a unique and surprising structural similarity to the amino-terminal domain of the helicase itself. In this minireview, the current data are discussed and important new structural and functional aspects of the helicase-primase interaction are highlighted. An attractive structural model with direct biological significance for the function of this complex and also for the development of new antibacterial compounds is examined.