Yatakemycin biosynthesis requires two deoxyribonucleases for toxin self-resistance.

The highly active natural product yatakemycin (YTM) from sp. TP-A0356 is a potent DNA damaging agent with antimicrobial and antitumor properties. The YTM biosynthesis gene cluster () contains several toxin self-resistance genes.

Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP) endonuclease activity.

TatD enzymes are evolutionarily conserved deoxyribonucleases associated with DNA repair, apoptosis, development, and parasite virulence. Three TatD paralogs exist in humans, but their nuclease functions are unknown. Here, we describe the nuclease activities of two of the three human TatD paralogs, TATDN1 and TATDN3, which represent two phylogenetically distinct clades based on unique active site motifs.

Mapping the deformability of natural and designed cellulosomes in solution.

Background: Natural cellulosome multi-enzyme complexes, their components, and engineered 'designer cellulosomes' (DCs) promise an efficient means of breaking down cellulosic substrates into valuable biofuel products. Their broad uptake in biotechnology relies on boosting proximity-based synergy among the resident enzymes, but the modular architecture challenges structure determination and rational design.

Results: We used small angle X-ray scattering combined with molecular modeling to study the solution structure of cellulosomal components.

Structural evolution of a DNA repair self-resistance mechanism targeting genotoxic secondary metabolites.

Microbes produce a broad spectrum of antibiotic natural products, including many DNA-damaging genotoxins. Among the most potent of these are DNA alkylating agents in the spirocyclopropylcyclohexadienone (SCPCHD) family, which includes the duocarmycins, CC-1065, gilvusmycin, and yatakemycin. The yatakemycin biosynthesis cluster in Streptomyces sp.

Structural and enzymatic characterisation of the Type III effector NopAA (=GunA) from Sinorhizobium fredii USDA257 reveals a Xyloglucan hydrolase activity.

Rhizobia are nitrogen-fixing soil bacteria that can infect legume plants to establish root nodules symbiosis. To do that, a complex exchange of molecular signals occurs between plants and bacteria. Among them, rhizobial Nops (Nodulation outer proteins), secreted by a type III secretion system (T3SS) determine the host-specificity for efficient symbiosis with plant roots.

Author Correction: Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Author Correction: Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis.

In the original version of this Article, the final concentration of riboflavin in the supplemented LB medium for recombinant LkcE expression was incorrectly stated as 1 g L (this was the concentration of the stock solution) and should have read 10-50 mg L-. This error has been corrected in both the PDF and HTML versions of the Article.

The laterally acquired GH5 EngA from the marine bacterium is dedicated to hemicellulose hydrolysis.

Cell walls of marine macroalgae are composed of diverse polysaccharides that provide abundant carbon sources for marine heterotrophic bacteria. Among them, is considered as a model for studying algae-bacteria interactions. The degradation of typical algal polysaccharides, such as agars or alginate, has been intensively studied in this model bacterium, but the catabolism of plant-like polysaccharides is essentially uncharacterized.

Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis.

Acquisition of new catalytic activity is a relatively rare evolutionary event. A striking example appears in the pathway to the antibiotic lankacidin, as a monoamine oxidase (MAO) family member, LkcE, catalyzes both an unusual amide oxidation, and a subsequent intramolecular Mannich reaction to form the polyketide macrocycle. We report evidence here for the molecular basis for this dual activity.

Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase.

Modular polyketide synthases (PKSs) direct the biosynthesis of clinically valuable secondary metabolites in bacteria. The fidelity of chain growth depends on specific recognition between successive subunits in each assembly line: interactions mediated by C- and N-terminal "docking domains" (DDs). We have identified a new family of DDs in trans-acyl transferase PKSs, exemplified by a matched pair from the virginiamycin (Vir) system.