Search for: All records

Abstract Despite technological advances over the last several decades, ship-based hydrography remains the only method for obtaining high-quality, high spatial and vertical resolution measurements of physical, chemical, and biological parameters over the full water column essential for physical, chemical, and biological oceanography and climate science. The Global Ocean Ship-based Hydrographic Investigations Program (GO-SHIP) coordinates a network of globally sustained hydrographic sections. These data provide a unique data set that spans four decades, comprised of more than 40 cross-ocean transects. The section data are, however, difficult to use owing to inhomogeneous format. The purpose of this new temperature, salinity, and dissolved oxygen data product is to combine, reformat and grid these data measured by Conductivity-Temperature-Depth-Oxygen (CTDO) profilers in order to facilitate their use by a wider audience. The product is machine readable and readily accessible by many existing visualisation and analysis software packages. The data processing can be repeated with modifications to suit various applications such as analysis of deep ocean, validation of numerical simulation, and calibration of autonomous platforms. 

Summary The Crp/Fnr family of transcriptional regulators play central roles in transcriptional control of diverse physiological responses, and are activated by a surprising diversity of mechanisms. MrpC is a Crp/Fnr homolog that controls theMyxococcus xanthusdevelopmental program. A long‐standing model proposed that MrpC activity is controlled by the Pkn8/Pkn14 serine/threonine kinase cascade, which phosphorylates MrpC on threonine residue(s) located in its extreme amino‐terminus. In this study, we demonstrate that a stretch of consecutive threonine and serine residues, T₂₁T₂₂S₂₃S_24,is necessary for MrpC activity by promoting efficient DNA binding. Mass spectrometry analysis indicated the TTSS motif is not directly phosphorylated by Pkn14in vitrobut is necessary for efficient Pkn14‐dependent phosphorylation on several residues in the remainder of the protein. In an important correction to a long‐standing model, we show Pkn8 and Pkn14 kinase activities do not play obvious roles in controlling MrpC activity in wild‐typeM. xanthusunder laboratory conditions. Instead, we propose Pkn14 modulates MrpC DNA binding in response to unknown environmental conditions. Interestingly, substitutions in the TTSS motif caused developmental defects that varied between biological replicates, revealing that MrpC plays a role in promoting a robust developmental phenotype.