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<jats:title>A plant-herbivore information “arms race”</jats:title> <jats:p> The consumption of plants by herbivores has driven the evolution of many diverse plant defense chemicals to which herbivores have constantly adapted. The transmission of chemical information at the community level is less known but important given the plethora of plant and herbivore species, especially in tropical communities. Zu <jats:italic>et al.</jats:italic> propose an information “arms race” approach to explain plant-herbivore chemical communication at the community level (see the Perspective by Solé). To test their conceptual framework, they used field data of herbivore-plant interactions and plant–volatile organic compound associations in a tropical dry forest. Their approach provides an understanding of the functioning and persistence of systems where individuals send and receive information in the form of signals to which other individuals react and, in turn, affect the behavior of other participants in these systems. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6497" page="1377" related-article-type="in-this-issue" vol="368" xlink:href="10.1126/science.aba2965">1377</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6497" page="1315" related-article-type="in-this-issue" vol="368" xlink:href="10.1126/science.abc6344">1315</jats:related-article> </jats:p>

<jats:title>Delicate dance becomes a ballet</jats:title> <jats:p> The enzyme nitrogenase uses adenosine triphosphate and several unusual iron-sulfur cofactors to pump electrons into typically inert dinitrogen (N <jats:sub>2</jats:sub> ), providing protons along the way. Previous work has shown that sulfur atoms in the iron-molybdenum cofactor (FeMoCo) are labile and suggests that replacement of one of the sulfurs by N <jats:sub>2</jats:sub> is integral to the mechanism of N <jats:sub>2</jats:sub> binding and reduction. Through the elimination of excess reducing agent during preparation, Kang <jats:italic>et al.</jats:italic> determined structures of Mo-nitrogenase in a resting conformation. Unexpectedly, they found that all three sulfurs at the outer edge of FeMoCo appear to be labile, with one subunit even having two of three sulfurs replaced by light, diatomic ligands. Biochemical and spectroscopic data indicate that the protein is active, holds tightly bound N <jats:sub>2</jats:sub> , and is in the expected oxidation state. These results may prompt a reassessment of the possible mechanisms of N <jats:sub>2</jats:sub> reduction and the role of dynamic belt ligands in FeMoCo. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6497" page="1381" related-article-type="in-this-issue" vol="368" xlink:href="10.1126/science.aaz6748">1381</jats:related-article> </jats:p>

<jats:title>Drug partitioning in nuclear condensates</jats:title> <jats:p> There is increasing interest in the function of phase-separated biomolecular condensates in cells because of their distinct properties and expanding roles in important biological processes. Klein <jats:italic>et al.</jats:italic> considered the fate of small-molecule therapeutics in the context of nuclear condensates (see the Perspective by Viny and Levine). They show that certain antineoplastic drugs have physicochemical properties that cause them to concentrate preferentially in condensates, both in vitro and in cancer cells. This property influences drug activity, and protein mutations that alter condensate formation can lead to drug resistance. Optimizing condensate partitioning may be valuable in developing improved therapeutics. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6497" page="1386" related-article-type="in-this-issue" vol="368" xlink:href="10.1126/science.aaz4427">1386</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6497" page="1314" related-article-type="in-this-issue" vol="368" xlink:href="10.1126/science.abc5318">1314</jats:related-article> </jats:p>