“Other” possibilities? Assessing regional and extra-regional dental affinities of populations in the Portuguese Estremadura to explore the roots of Iberia’s Late Neolithic-Copper Age

The relationship between the development of social complexity in the Iberian Peninsula during the 4th and 3rd millennia BCE (Late Neolithic and Copper Age) and population movement has been a longstanding question. Biological affinity analyses were used to explore Iberian demographic dynamics, and specifically, to discern whether there is evidence for migration and gene flow between northwest African, eastern Mediterranean, and Iberian populations. Affinities based on comparisons of nonmetric traits from the Arizona State University Dental Anthropology System were estimated among samples of burial populations from three key Late Neolithic-Copper Age sites in the Portuguese Estremadura: Cova da Moura (3700-2300 BCE), Bolores (2800-2600 BCE), and Pai Mogo I (2800-2600 BCE). Results indicate: 1) the possibility of genetic exchange with African and other Mediterranean peoples, 2) some measure of population continuity over time in the Estremadura, and 3) possible local isolation of populations, given distinctive patterning at the site of Pai Mogo, located 23 km north of Cova da Moura and Bolores

Inhibition of Bacterial Ice Nucleators Is Not an Intrinsic Property of Antifreeze Proteins

Cold-adapted organisms use antifreeze proteins (AFPs) or ice-nucleating proteins (INPs) for the survival in freezing habitats. AFPs have been reported to be able to inhibit the activity of INPs, a property that would be of great physiological relevance. The generality of this effect is not understood, and for the few known examples of INP inhibition by AFPs, the molecular mechanisms remain unclear. Here, we report a comprehensive evaluation of the effects of five different AFPs on the activity of bacterial ice nucleators using a high-throughput ice nucleation assay. We find that bacterial INPs are inhibited by certain AFPs, while others show no effect. Thus, the ability to inhibit the activity of INPs is not an intrinsic property of AFPs, and the interactions of INPs and different AFPs proceed through protein-specific rather than universal molecular mechanisms