Dissecting Bottromycin Biosynthesis Using Comparative Untargeted Metabolomics.

Bottromycin A2 is a structurally unique ribosomally synthesized and post-translationally modified peptide (RiPP) that possesses potent antibacterial activity towards multidrug-resistant bacteria. The structural novelty of bottromycin stems from its unprecedented macrocyclic amidine and rare β-methylated amino acid residues. The N-terminus of a precursor peptide (BtmD) is converted into bottromycin A2 by tailoring enzymes encoded in the btm gene cluster.

The effect of Parkinson's-disease-associated mutations on the deubiquitinating enzyme UCH-L1.

The neuronal ubiquitin C-terminal hydrolase (UCH) UCH-L1 has been linked to Parkinson's disease (PD) and other neurodegenerative diseases. Here, we present a study on the structure, stability, unfolding, and dynamics of wild-type and mutant UCH-L1. Fluorescence, far-UV CD, and NMR measurements were used to establish that the unfolding of UCH-L1 is three-state under equilibrium conditions and that an intermediate is populated.