Kenneth J. McDowall

TL;DR: This review is peppered with approaches that may expand the screening of streptomycetes for new antibiotics by awakening expression of cryptic antibiotic biosynthetic genes.

TL;DR: In this article, the crystal structures of the catalytic domain of RNase E as trapped allosteric intermediates with RNA substrates are reported, and the structure explains how the recognition of the 5' terminus of the substrate may trigger catalysis and also sheds light on the question of selectively process, rather than destroy, specific RNA precursors.

TL;DR: It is found that the precise point of RNase E cleavage can be altered specifically and reproducibly by sequence changes in the region cleaved and, therefore, is not determined by a distance measured in nucleotides from any other sequence or region of secondary structure in RNA I.

TL;DR: The results, which map the catalytic domain of RNase E, indicate the existence of discrete functional domains within the multifaceted Rne protein.

TL;DR: An update of the review of the Streptomycetaceae, a family of Gram-positive bacteria that inhabit both soil and aquatic sediments, focuses on recent developments in the understanding of the underlying regulatory networks, ecological triggers of natural product biosynthesis, contributions from comparative genomics and approaches to awaken the biosynthesis of otherwise silent or cryptic natural products.