Cross-shelf mixing and mid-shelf front dynamics in the Mid-Atlantic Bight evaluated using the radium quartet

Mid-shelf fronts (MSFs) are thought to be ubiquitous in shelf areas. However, their dynamical role in cross-shelf mixing has yet to be fully characterized. In January, February, and April of 2007, radium isotopes (223Ra, t1/2 = 11 d; 224Ra, t1/2 = 3.7 d; 226Ra, t1/2 = 1600 yr; 228Ra, t1/2 = 5.7 yr) were measured along a transect in the Mid-Atlantic Bight to constrain mixing rates at and around a MSF. Cross-shelf eddy diffusivities (Kx) were determined from 223Ra and 224Ra distributions using a variable-depth model. Two key assumptions – minimal advection and negligible benthic radium input – involving the use of 223Ra and 224Ra as tracers of mixing were quantitatively evaluated in order to assess the accuracy of the Kx estimates. Eddy diffusivities over the three-month sampling period range from 0.1 ± 0.05 – 1.6 ± 0.5 × 102 m2 s–1 for 223Ra and from 1.7 ± 0.4 – 2.2 ± 0.6 × 102 m2 s–1 for 224Ra. The temporal variability in Kx is low in comparison to the uncertainty of the derived values, indicating that eddy diffusivity in this area is relatively constant throughout the sampling period. Observations in the Mid-Atlantic Bight differ from theoretical data corresponding to the tidal dispersion frontogenesis model, suggesting that a different mechanism is responsible for MSF formation. Variability in supported 223Ra and 228Ra observed near the front indicates that cross-shelf mixing may be inhibited by MSFs. Conversely, along-shelf transport is enhanced by the front\u27s presence. These results indicate that the equatorward jet associated with the front is capable of effectively transporting dissolved chemicals over hundreds of kilometers

Structure of a Eukaryotic Nonribosomal Peptide Synthetase Adenylation Domain That Activates a Large Hydroxamate Amino Acid in Siderophore Biosynthesis*

Nonribosomal peptide synthetases (NRPSs) are large, multidomain proteins that are involved in the biosynthesis of an array of secondary metabolites. We report the structure of the third adenylation domain from the siderophore-synthesizing NRPS, SidN, from the endophytic fungus Neotyphodium lolii. This is the first structure of a eukaryotic NRPS domain, and it reveals a large binding pocket required to accommodate the unusual amino acid substrate, Nδ-cis-anhydromevalonyl-Nδ-hydroxy-l-ornithine (cis-AMHO). The specific activation of cis-AMHO was confirmed biochemically, and an AMHO moiety was unambiguously identified as a component of the fungal siderophore using mass spectroscopy. The protein structure shows that the substrate binding pocket is defined by 17 amino acid residues, in contrast to both prokaryotic adenylation domains and to previous predictions based on modeling. Existing substrate prediction methods for NRPS adenylation domains fail for domains from eukaryotes due to the divergence of their signature sequences from those of prokaryotes. Thus, this new structure will provide a basis for improving prediction methods for eukaryotic NRPS enzymes that play important and diverse roles in the biology of fungi