The histone variant H2AZ marks nucleosomes flanking the promoters of most genes of budding yeast. The incorporation of H2AZ into chromatin is dependent on the SWR1 complex, which catalyses the replacement of conventional histone H2A with H2AZ. In cells, the pool of unincorporated histone H2AZ has previously been found in association with Nap1, a chaperone for conventional histone H2A-H2B. Here, we report the discovery of Chz1, a histone chaperone that has preference for H2AZ and can also deliver a source of the histone variant for SWR1-dependent histone replacement. Bacterially expressed Chz1 forms a heterotrimer with H2AZ-H2B, stabilizing the association of the histone dimer. We have identified a conserved motif important for histone variant recognition within the H2AZ-interacting domain of Chz1. The presence of this motif in other metazoan proteins suggests that H2AZ-specific chaperones may be widely conserved.

This study defined normal motion of the syndesmosis and the biomechanical consequences of injury. The degree of instability was increased with each additional injured structure; however, isolated injuries to the AITFL alone may lead to significant external rotary instability.

Constructs were comparable across most conditions; however, when repairing injuries with a suture-button construct, a single suture-button construct may not provide sufficient resistance to sagittal translation of the fibula.