Animals employ a variety of behaviors to reduce or manage predation risk. Often, these are studied in isolation, but selection may act on packages of behavior that are referred to as behavioral syndromes. We focused on yellowbellied marmots (Marmota flaviventris) and examined three commonly studied antipredator behaviors. We fitted general linear models to explain variation in maximum running speed, time allocated to vigilance and foraging during bouts of foraging, and flight initiation distance (FID). Marmot maximum running speed was influenced by the substrate run across; marmots ran fastest across dirt or low vegetation and slowest across stones or talus. Incline and several other variables shown to affect running speed in other marmot species failed to explain significant variation in yellow-bellied marmots. From these results we expected marmots to be sensitive to substrate while foraging, but insensitive to incline. However, time allocated to foraging was affected by incline but not by substrate. In bouts of foraging observed in different habitats, and on different inclines, more time was allocated to foraging and less to vigilance on steep slopes and less on level ground. Substrate influenced FID. Marmots in tall vegetation were less tolerant of an approaching person than were those in shorter vegetation. Finally, we found significant correlations between the residuals from the maximum running speed model and the residuals from the time allocated to vigilance and foraging models. We found a tendency for marmots that ran slower than predicted to be less vigilant while foraging. We also found that relatively slow marmots engaged in more active foraging and less vigilance during foraging bouts. This finding suggests a Ôlocomotor abilitywariness while foragingÕ syndrome. It also suggests that vulnerable individuals minimize their exposure while foraging.
Disulfide bond forming (Dsb) proteins ensure correct folding and disulfide bond formation of secreted proteins. Previously, we showed that Mycobacterium tuberculosis DsbE (Mtb DsbE, Rv2878c) aids in vitro oxidative folding of proteins. Here we present structural, biochemical and gene expression analyses of another putative Mtb secreted disulfide bond isomerase protein homologous to Mtb DsbE, Mtb DsbF (Rv1677). The X-ray crystal structure of Mtb DsbF reveals a conserved thioredoxin fold although the active-site cysteines may be modeled in both oxidized and reduced forms, in contrast to the solely reduced form in Mtb DsbE. Furthermore, the shorter loop region in Mtb DsbF results in a more solvent-exposed active site. Biochemical analyses show that, similar to Mtb DsbE, Mtb DsbF can oxidatively refold reduced, unfolded hirudin and has a comparable pKa for the active-site solvent-exposed cysteine. However, contrary to Mtb DsbE, the Mtb DsbF redox potential is more oxidizing and its reduced state is more stable. From computational genomics analysis of the M. tuberculosis genome, we identified a potential Mtb DsbF interaction partner, Rv1676, a predicted peroxiredoxin. Complex formation is supported by protein co-expression studies and inferred by gene expression profiles, whereby Mtb DsbF and Rv1676 are upregulated under similar environments. Additionally, comparison of Mtb DsbF and Mtb DsbE gene expression data indicate anticorrelated gene expression patterns, suggesting that these two proteins and their functionally linked partners constitute analogous pathways that may function under different conditions.
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