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Researchers and policy makers increasingly recognize the need to adapt to future changes in climate, given that past emissions of greenhouse gases have already committed the world to some level of climate change. However, the current understanding of the costs and benefits of adaptation measures is still fairly rudimentary, and far from comprehensive. An assessment is presented of the current state of knowledge on the magnitude of adaptation costs in the United States. While incomplete, the studies suggest that adaptation cost could be as high as tens or hundreds of billions of dollars per year by the middle of this century. Key studies are identified in each sector, and the cost estimates and approaches to cost estimation are surveyed. Methodological issues are highlighted in interpreting, comparing, and aggregating adaptation cost estimates. Policy recommendations are made along with appropriate steps to make future adaptation cost studies more comparable within and across sectors and more accessible and relevant to policy and decision makers. Policy relevance Designing and implementing climate change adaptation policy requires good information about the effectiveness and cost of available adaptive options. The current state of knowledge on adaptation costs in the United States is assessed and significant gaps in the literature are highlighted – particularly in terms of sectoral and geographic coverage – as well as inconsistencies in methodologies and assumptions that hamper comparison across studies. Critical steps are identified that can be taken to make adaptation cost studies more accessible and useful to decision makers. The findings and recommendations are relevant to adaptation cost studies globally, not just in the United States. [ABSTRACT FROM AUTHOR]

The translational GTPases promote initiation, elongation, and termination of protein synthesis by interacting with the ribosome. Mutations that impair GTP hydrolysis by eukaryotic translation initiation factor 5B/initiation factor 2 (eIF5B/IF2) impair yeast cell growth due to failure to dissociate from the ribosome following subunit joining. A mutation in helix h5 of the 18S rRNA in the 40S ribosomal subunit and intragenic mutations in domain II of eIF5B suppress the toxic effects associated with expression of the eIF5B-H480I GTPase-deficient mutant in yeast by lowering the ribosome binding affinity of eIF5B. Hydroxyl radical mapping experiments reveal that the domain II suppressors interface with the body of the 40S subunit in the vicinity of helix h5. As the helix h5 mutation also impairs elongation factor function, the rRNA and eIF5B suppressor mutations provide in vivo evidence supporting a functionally important docking of domain II of the translational GTPases on the body of the small ribosomal subunit. [ABSTRACT FROM AUTHOR]