: Direct and indirect effects of industrial development have contributed, in part, to the threatened status of boreal ecotype caribou (Rangifer tarandus caribou) in Alberta and Canada. Our goal was to develop a model that would allow managers to identify landscape‐scale targets for industrial development, while ensuring functional habitat for sustainable caribou populations. We examined the relationship between functional habitat loss resulting from cumulative effects of natural and anthropogenic disturbance, and the rate of population change (Λ) for 6 populations of boreal caribou in Alberta, Canada. We defined functional habitat loss according to 2 variables for which we had a priori reasons to suspect causative associations with Λ: 1) percentage area of caribou range within 250 m of anthropogenic footprint, and 2) percentage of caribou range disturbed by wildfire within the last 50 years. Multiple regression coefficients for both independent variables indicated significant effects on Λ. The 2‐predictor model explained 96% (R2) of observed variation in Λ among population units (F2,3 = 35.2, P = 0.008). The model may be used to evaluate plans for industrial development in relation to predicted wildfire rates and goals for caribou population growth rates.

Centromere protein A (CENP-A) is a histone H3 variant that marks centromere location on the chromosome. To study the subunit structure and folding of human CENP-A-containing chromatin, we generated a set of nucleosomal arrays with canonical core histones and another set with CENP-A substituted for H3. At the level of quaternary structure and assembly, we find that CENP-A arrays are composed of octameric nucleosomes that assemble in a stepwise mechanism, recapitulating conventional array assembly with canonical histones. At intermediate structural resolution, we find that CENP-A-containing arrays are globally condensed relative to arrays with the canonical histones. At high structural resolution, using hydrogen-deuterium exchange coupled to mass spectrometry (H/DX-MS), we find that the DNA superhelical termini within each nucleosome are loosely connected to CENP-A, and we identify the key amino acid substitution that is largely responsible for this behavior. Also the C terminus of histone H2A undergoes rapid hydrogen exchange relative to canonical arrays and does so in a manner that is independent of nucleosomal array folding. These findings have implications for understanding CENP-A-containing nucleosome structure and higher-order chromatin folding at the centromere.hydrogen exchange | epigenetics

The responses of a herd of migratory woodland caribou (Rangifer tarandus caribou) to timber harvesting that fragmented about 11% of their winter range in west-central Alberta were examined in this study. From 1981 to 1996, 45 caribou were radio-collared and monitored during the initiation and completion of first-pass timber harvest (50% removal). Variables examined were home-range size, daily movement rates, and distance to the nearest cut block for radio-collared individuals. Daily movement rates and individual winter range sizes decreased as timber harvesting progressed. Caribou avoided using recently fragmented areas by an average of 1.2 km. If fragmentation of the winter range continues through timber harvesting and other industrial activities, the "spacing out" antipredator strategy used by caribou may be compromised. Based on these findings, timber-harvesting strategies are recommended that (i) ensure an adequate area of usable habitat to support the current population, (ii) minimize the amount of fragmented area, and (iii) in the short term avoid presently defined core use areas.

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Mg2؉ -dependent oligomerization of nucleosomal arrays is correlated with higher order folding transitions that stabilize chromosome structure beyond the 30-nm diameter fiber. In the present studies, we have employed a novel mutagenesis-based approach to identify the macromolecular determinants that control H4 N-terminal domain (NTD) function during oligomerization. Core histones were engineered in which 1) the H2A, H2B, and H3 NTDs were swapped onto the H4 histone fold; 2) the length of the H4 NTD and the H2A NTD on the H4 histone fold, were increased; 3) the charge density of the NTDs on the H4 histone fold was increased or decreased; and 4) the H4 NTD was placed on the H2B histone fold. Model nucleosomal arrays were assembled from wild type and mutant core histone octamers, and Mg 2؉ -dependent oligomerization was characterized. The results demonstrated that the H2B and H3 NTDs could replace the H4 NTD, as could the H2A NTD if it was duplicated to the length of the native H4 NTD. Arrays oligomerized at lower salt concentrations as the length of the NTD on the H4 histone fold was increased. Mutations that decreased the NTD charge density required more Mg 2؉ to oligomerize, whereas mutants that increased the charge density required less salt. Finally, the H4 NTD functioned differently when attached to the H2B histone fold than the H4 histone fold. These studies have revealed new insights into the biochemical basis for H4 NTD effects on genome architecture as well as the protein chemistry that underlies the function of the intrinsically disordered H4 NTD.