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The cover shows a ~50xâ light micrograph of a growing colony of Mycobacterium tuberculosis, the causative agent of human tuberculosis. Bertozzi and colleagues have identified and solved the structure of the sulfotransferase that initiates the biosynthesis of a major component of the cell wall implicated in virulence. The intricate, snake-like threedimensional projections of these colonies have been attributed to components of the cell wall. See pp 721-724; News and Views pp 686-687.
In a spectacular location nestled in the hills on Croatia's coast, a group of ∼300 scientists from around the world gathered to listen to recent advances in cellular signaling and to gaze across the Adriatic Sea during discussions that surely put this work into perspective. Topics discussed ranged from precise structural details of signaling events to animal models for understanding signaling disorders.
The key step in the biosynthesis of a sulfated glycolipid in the disease-causing bacterium Mycobacterium tuberculosis is revealed by the discovery of the sulfotransferase that installs the sulfate moiety.
Structures of the human O6-alkylguanine-DNA alkyltransferase bound to substrate together with biochemical analysis provide clues to substrate acquisition and recognition, as well as details of the methyl transfer reaction catalyzed by this direct DNA repair protein.
Recent studies on the metabotropic glutamate receptors provide new insights into their signaling mechanisms that may apply to other G-protein coupled receptor (GPCR) families.
Mus81-Eme1 is a structure-specific DNA endonuclease complex that processes DNA junctions during the recombinational repair of DNA damage. The recent observation that mice containing disruptions in one or both copies of the MUS81 gene are profoundly cancer prone demonstrates that efficient processing of recombination intermediates is necessary to guard against tumorigenesis.