A New Type of Proton Coordination in an F1Fo-ATP Synthase Rotor Ring

The high-resolution structure of the rotor ring from alkaliphilic Bacillus pseudofirmus OF4 reveals a new type of ion binding in F1Fo-ATP synthases

Low pH enhances the action of maximin H5 against Staphylococcus aureus and helps mediate lysylated phosphatidylglycerol induced resistance

Maximin H5 (MH5) is an amphibian antimicrobial peptide specifically targeting Staphylococcus aureus. At pH 6, the peptide showed an increased ability to penetrate (∆П = 6.2 mN m-1) and lyse (lysis = 48 %) S. aureus membrane mimics, which incorporated physiological levels of lysylated phosphatidylglycerol (Lys-PG, 60 %) as compared to pH 7 (∆П = 5.6 mN m-1 and lysis = 40 % at pH 7) where levels of Lys-PG are lower (40 %). The peptide therefore appears to have optimal function at pH levels known to be optimal for the organism’s growth. MH5 killed S. aureus (minimum inhibitory concentration = 90 µM) via membranolytic mechanisms that involved the stabilization of α-helical structure (circa 45-50 %) and which showed similarities to the ‘Carpet’ mechanism based on its ability to increase the rigidity (Cs-1 = 109.94 mN m-1) and thermodynamic stability (∆Gmix = -3.0) of physiologically relevant S. aureus membrane mimics at pH 6. Based on theoretical analysis this mechanism may involve the use of a tilted peptide structure and efficacy was noted to vary inversely with the Lys-PG content of S. aureus membrane mimics for each pH studied (R2 circa 0.97), which led to the suggestion that under biologically relevant conditions, low pH helps mediate Lys-PG induced resistance in S. aureus to MH5 antibacterial action. The peptide showed a lack of haemolytic activity (< 2 % haemolysis) and merits further investigation as a potential template for development as an anti-staphylococcal agent in medically and biotechnically relevant areas

Genomics of alkaliphiles

Alkalinicity presents a challenge for life due to a “reversed” proton gradient that is unfavourable to many bioenergetic processes across the membranes of microorganisms. Despite this, many bacteria, archaea, and eukaryotes, collectively termed alkaliphiles, are adapted to life in alkaline ecosystems and are of great scientific and biotechnological interest due to their niche specialization and ability to produce highly stable enzymes. Advances in next-generation sequencing technologies have propelled not only the genomic characterization of many alkaliphilic microorganisms that have been isolated from nature alkaline sources but also our understanding of the functional relationships between different taxa in microbial communities living in these ecosystems. In this review, we discuss the genetics and molecular biology of alkaliphiles from an “omics” point of view, focusing on how metagenomics and transcriptomics have contributed to our understanding of these extremophiles.https://link.springer.com/bookseries/10hj2021BiochemistryGeneticsMicrobiology and Plant Patholog

A trehalose biosynthetic enzyme doubles as an osmotic stress sensor to regulate bacterial morphogenesis

The dissacharide trehalose is an important intracellular osmoprotectant and the OtsA/B pathway is the principal pathway for trehalose biosynthesis in a wide range of bacterial species. Scaffolding proteins and other cytoskeletal elements play an essential role in morphogenetic processes in bacteria. Here we describe how OtsA, in addition to its role in trehalose biosynthesis, functions as an osmotic stress sensor to regulate cell morphology in Arthrobacter strain A3. In response to osmotic stress, this and other Arthrobacter species undergo a transition from bacillary to myceloid growth. An otsA null mutant exhibits constitutive myceloid growth. Osmotic stress leads to a depletion of trehalose-6-phosphate, the product of the OtsA enzyme, and experimental depletion of this metabolite also leads to constitutive myceloid growth independent of OtsA function. In vitro analyses indicate that OtsA can self-assemble into protein networks, promoted by trehalose-6-phosphate, a property that is not shared by the equivalent enzyme from E. coli, despite the latter's enzymatic activity when expressed in Arthrobacter. This, and the localization of the protein in non-stressed cells at the mid-cell and poles, indicates that OtsA from Arthrobacter likely functions as a cytoskeletal element regulating cell morphology. Recruiting a biosynthetic enzyme for this morphogenetic function represents an intriguing adaptation in bacteria that can survive in extreme environments

The design and evaluation of EKE, a semi-automated email knowledge extraction tool

This is a post-peer-review, pre-copyedit version of an article published in Knowledge Management Research and Practice. The definitive publisher-authenticated version, TEDMORI, S. and JACKSON, T., 2012. The design and evaluation of EKE, a semi-automated email knowledge extraction tool. Knowledge Management Research and Practice, 10 (1), pp. 79 - 88 is available online at: http://dx.doi.org/10.1057/kmrp.2011.40This paper presents an approach to locating experts within organisations through the use of the indispensable communication medium and source of information, email. The approach was realised through the email expert locator architecture developed by the authors, which uses email content in the modelling of individuals' expertise profiles. The approach has been applied to a real-world application, EKE, and evaluated using focus group sessions and system trials. In this work, the authors report the findings obtained from the focus groups sessions. The aim of the sessions was to obtain information about the participants' perceptions, opinions, underlying attitudes, and recommendations with regard to the notion of exploiting email content for expertise profiling. The paper provides a review of the various approaches to expertise location that have been developed and highlights the end-users' perspectives on the usability and functionality of EKE and the socio-ethical challenges raised by its adoption from an industrial perspective. © 2012 Operational Research Society. All rights reserved