Quantifying the nutritional quality of forage fish is integral for understanding upper trophic levels as forage fish are the dominant prey for top predator fish, marine mammals, and sea birds. Many existing reports documenting body composition of forage species are not comparable due to confounding effects. This study systematically assessed the variability in proximate composition and energy content of 16 forage species in southeastern Alaska (57.2626 N/133.7394 W) between 2001 and 2004. Variation in energy and lipid contents was related to habitat, epipelagic planktivores varying most, mesopelagics intermediate, and demersal species relatively invariable. Season was the greatest source of variation as a result of short growing seasons at high latitude and energy allocation strategies for reproduction and growth. Among species that varied seasonally, energy and lipid increased over summer and declined during winter. Annual differences in body composition occurred during periods of peak energy content. Sampling recommendations and guidance for bioenergetics models are provided.Electronic supplementary materialThe online version of this article (doi:10.1007/s00227-010-1569-3) contains supplementary material, which is available to authorized users.

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The region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site. We have used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms a compact domain consisting of three antiparallel strands that contact A-T base pairs in the major groove. The three-strand domain is a novel fold among all known DNA-binding proteins. The PAR shares sequence homology with the N-terminal regions of other zinc finger proteins, suggesting that it represents a new DNA-binding module that extends the binding repertoire of zinc finger proteins.