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Humans are well-versed in reasoning about the behaviors of physical objects and choosing actions accordingly to accomplish tasks, while it remains a major challenge for AI. To facilitate research addressing this problem, we propose a new testbed that requires an agent to reason about physical scenarios and take an action appropriately. Inspired by the physical knowledge acquired in infancy and the capabilities required for robots to operate in real-world environments, we identify 15 essential physical scenarios. We create a wide variety of distinct task templates, and we ensure all the task templates within the same scenario can be solved by using one specific strategic physical rule. By having such a design, we evaluate two distinct levels of generalization, namely the local generalization and the broad generalization. We conduct an extensive evaluation with human players, learning agents with varying input types and architectures, and heuristic agents with different strategies. Inspired by how human IQ is calculated, we define the physical reasoning quotient (Phy-Q score) that reflects the physical reasoning intelligence of an agent using the physical scenarios we considered. Our evaluation shows that 1) all agents are far below human performance, and 2) learning agents, even with good local generalization ability, struggle to learn the underlying physical reasoning rules and fail to generalize broadly. We encourage the development of intelligent agents that can reach the human level Phy-Q score. Website: https://github.com/phy-q/benchmark, For the associated website, see https://github.com/phy-q/benchmark

Ribosomal protein L1 has a dual function as a ribosomal protein binding 23S rRNA and as a translational repressor binding its mRNA. L1 is a two-domain protein with N- and C-termini located in domain I. Earlier it was shown that L1 interacts with the same targets on both rRNA and mRNA mainly through domain I. We have suggested that domain I is necessary and sufficient for specific RNA-binding by L1. To test this hypothesis, a truncation mutant of L1 from Thermus thermophilus, representing domain I, was constructed by deletion of the central part of the L1 sequence, which corresponds to domain II. It was shown that the isolated domain I forms stable complexes with specific fragments of both rRNA and mRNA. The crystal structure of the isolated domain I was determined and compared with the structure of this domain within the intact protein L1. This comparison revealed a close similarity of both structures. Our results confirm our suggestion that in protein L1 its domain I alone is sufficient for specific RNA binding, whereas domain II stabilizes the L1-rRNA complex.

The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA-protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA-protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.