Liam M. Longo

Stunning views and exciting talks at the Annual Meeting of the Biophysical Society of Japan. Check out my poster, describing a project in collaboration with the Prof. Norman Metanis and Prof. Koby Levy, here!

Although OIST is surrounded by stunning beaches, the real draw is the cutting-edge research happening on campus. Thanks so much to fellow Tawfik Lab alumnus Prof. Paola Laurino for inviting me!

Anthropogenic organophosphorus compounds (AOPCs), such as phosphotriesters, are used extensively as plasticizers, flame retardants, nerve agents, and pesticides. To date, only a handful of soil bacteria bearing a phosphotriesterase (PTE), the key enzyme in the AOPC degradation pathway, have been identified. Therefore, the extent to which bacteria are capable of utilizing AOPCs as a phosphorus source, and how widespread this adaptation may be, remains unclear. Marine environments with phosphorus limitation and increasing levels of pollution by AOPCs may drive the emergence of PTE activity. Here, we report the utilization of diverse AOPCs by four model marine bacteria and 17 bacterial isolates from the Mediterranean Sea and the Red Sea. To unravel the details of AOPC utilization, two PTEs from marine bacteria were isolated and characterized, with one of the enzymes belonging to a protein family that, to our knowledge, has never before been associated with PTE activity. When expressed in Escherichia coli with a phosphodiesterase, a PTE isolated from a marine bacterium enabled growth on a pesticide analog as the sole phosphorus source. Utilization of AOPCs may provide bacteria a source of phosphorus in depleted environments and offers a prospect for the bioremediation of a pervasive class of anthropogenic pollutants.

Peptide-RNA coacervates can result in the concentration and compartmentalization of simple biopolymers. Given their primordial relevance, peptide-RNA coacervates may have also been a key site of early protein evolution. However, the extent to which such coacervates might promote or suppress the exploration of novel peptide conformations is fundamentally unknown. To this end, we used electron paramagnetic resonance spectroscopy (EPR) to characterize the structure and dynamics of an ancient and ubiquitous nucleic acid binding element, the helix-hairpin-helix (HhH) motif, alone and in the presence of RNA, with which it forms coacervates. Double electron–electron resonance (DEER) spectroscopy applied to singly labeled peptides containing one HhH motif revealed the presence of dimers, even in the absence of RNA. Moreover, dimer formation is promoted upon RNA binding and was detectable within peptide-RNA coacervates. DEER measurements of spin-diluted, doubly labeled peptides in solution indicated transient α-helical character. The distance distributions between spin labels in the dimer and the signatures of α-helical folding are consistent with the symmetric (HhH)2-Fold, which is generated upon duplication and fusion of a single HhH motif and traditionally associated with dsDNA binding. These results support the hypothesis that coacervates are a unique testing ground for peptide oligomerization and that phase-separating peptides could have been a resource for the construction of complex protein structures via common evolutionary processes, such as duplication and fusion.

The Blue Marble Space Institute of Science (BMSIS) is an international group of scientists interested in basic science, sustainability, and public engagement. I can't wait to start learning together with the kindred sprints at BMSIS!

At the IdeasLab, I had the opportunity to work alongside computer scientists and physicists as we developed projects to probe the nature of mind, agency, and the process of abiogenesis. Many thanks to the John Templeton Foundation for making this trip possible -- I learned so much from my peers and mentors, and it's a week I won't soon forget!

Check out made-for-YouTube versions of the talks here. As these papers are not yet published, the stories are subject to change! A collaboration between my lab and the Metanis Lab (Hebrew University of Jerusalem) about "ambidextrous" protein folds: A peek at some conversations between me and my former Postdoctoral Advisor Shawn McGlynn: