A novel marine bacterium, strain JCS350T, was isolated from marine sediment samples collected from a cold-seep area. The 16S rRNA gene sequence of the isolate showed high similarity to that of Erythrobacter luteolus SW-109T (95.9 % sequence similarity). Lower 16S rRNA gene sequence similarities were shown to other members of the genus Erythrobacter (94.6–95.4 %) and members of the genus Porphyrobacter (94.5–95.2 %). Phylogenetic analysis with all members of the family Erythrobacteraceae and several members of the family Sphingomonadaceae revealed that the isolate formed a phyletic line with [Erythrobacter] luteolus that was distinct from other members of the family Erythrobacteraceae. The dominant fatty acids of strain JCS350T were 18 : 1ω7c, 16 : 1ω7c and cyclopropane 17 : 0. The major respiratory quinone was ubiquinone 10. The DNA G+C content was 54.5 mol%. The isolate did not contain bacteriochlorophyll a. Optimal growth required the presence of 2 % (w/v) NaCl with either 0.18 % CaCl2 or 0.59 % MgCl2, at pH 6.5 and at 35 °C. On the basis of the evidence of this polyphasic taxonomic study, strain JCS350T should be classified in a novel genus and species in the family Erythrobacteraceae, for which the name Altererythrobacter epoxidivorans gen. nov., sp. nov. is proposed. The misclassified species [Erythrobacter] luteolus is transferred to the new genus as Altererythrobacter luteolus comb. nov. The type strain of Altererythrobacter epoxidivorans is JCS350T (=KCCM 42314T =JCM 13815T) and the type strain of Altererythrobacter luteolus is SW-109T (=KCTC 12311T =JCM 12599T).

Balancing act: The correct balance of electronic factors in the naphthazarin and isocoumarin fragments facilitates the acid‐mediated spiroketalization step to afford the key densely functionalized spiroketal (see picture; EOM=ethoxymethyl) in the formal synthesis of (±)‐γ‐rubromycin. A novel regioselective allyloxylation/Claisen rearrangement of 2‐azido‐1,4‐naphthoquinone provides access to the highly oxygenated naphthazarin fragment.

A psychrophilic bacterium, designated strain HJ039 T , was isolated from a marine sponge collected in the East Sea of Korea (also known as the Sea of Japan). Cells were . Growth was observed between 5 and 26 6C (optimum 15 6C), at pH 5?0-8?5 (optimum pH 6?0-6?5) and in the presence of 0-6?0 % NaCl (optimum 2?0 %). The 16S rRNA gene sequence of strain HJ039 T showed high levels of similarity (93?7-95?4 %) with members of the genus Shewanella, especially with Shewanella gaetbuli TF-27 T (95?2 %), Shewanella decolorationis S12 T (94?9 %), Shewanella putrefaciens LMG 26268 T (94?6 %), Shewanella hafniensis P010 T (94?6 %), Shewanella algae ATCC 51192 T (94?5 %) and Shewanella kaireitica c931 T (94?5 %). However, phylogenetic analysis revealed that strain HJ039 T shared a phyletic line with S. algae and Shewanella amazonensis. The major respiratory quinone was Q-8. The DNA G+C content was 52?8 mol%. The major fatty acids were i-13 : 0 (8?5 %), 15 : 0 (4?2 %), i-15 : 0 (23?2 %), i-15 : 1 (7?9 %), 16 : 0 (8?7 %), 16 : 1v7 (21?0 %) and 17 : 1v8 (6?4 %). From this polyphasic taxonomic evidence, strain HJ039 T is considered to represent a novel species of the genus Shewanella, for which the name Shewanella spongiae sp. nov. is proposed. The type strain is HJ039 T (=KCCM 42304 T =JCM 13830 T ).

Peptide and protein aberrant lipidation patterns are often involved in many diseases including cancer and neurological disorders. Peptide lipidation is also a promising strategy to improve pharmacokinetic and pharmacodynamic profiles of peptide-based drugs. Self-adjuvanting peptide-based vaccines commonly utilise the powerful TLR2 agonist PamCys lipid to stimulate adjuvant activity. The chemical synthesis of lipidated peptides can be challenging hence efficient, flexible and straightforward synthetic routes to access homogeneous lipid-tagged peptides are in high demand. A new technique coined Cysteine Lipidation on a Peptide or Amino acid (CLipPA) uses a 'thiol-ene' reaction between a cysteine and a vinyl ester and offers great promise due to its simplicity, functional group compatibility and selectivity. Herein a brief review of various synthetic strategies to access lipidated peptides, focusing on synthetic methods to incorporate a PamCys motif into peptides, is provided.

Replacing the O-linked saccharide in the bacteriocin glycocin F with an S-linked version results in a peptidomimetic that increases the bacteriostatic effect.