HG 195.45-195.55 Thin Section

Dark brown sediment with clasts ranging from small to large. The grains are sub-angular. Two main domains can be seen. Both are coarse grained, but one contains larger grains and potentially more clay material. Lineations are present throughout the sample in multiple directions. Minor rotation around a few larger clasts can be seen, as well as comet structures.

HG 215.65-215.75 Thin Section

Brown to dark brown sediment with small to medium sized clasts ranging from sub-angular to sub-rounded. This sample contains a coarse grained domain and a fine grained domain. Clear boundaries can be seen. Grain stacking can be seen in the coarse domain, while lineations are the dominant microstructure in the fine grained domain. Minor grain crushing can also be seen. Some of the coarser domain is rich in clay and organics.

HG 225.15-225.25 Thin Section

Dark brown sediment with sub-angular to sub-rounded grains, that range from small to medium in size. Lineations with fractured grains are abundant, and grain crushing can also be seen. Minor rotation can also be seen.

The structure of arabidopsis NPR1 : its function as a salicylic acid receptor and a metal-binding protein

The Arabidopsis NPRI protein regulates systemic acquired resistance dependent on salicylic acid. Analyses by plant two-hybrid analysis in vivo and pull-down assays in vitro showed that the BTB/POZ domain of NPRI at the N-terminus serves as an autoinhibitory domain to negate the function of the transactivation domain at the C-terminus through direct binding of these two domains. I t was also shown that the binding of the BTB/POZ domain to the C-terminus of NPRI was abolished by SA treatment, suggesting that SA could interfere directly with this binding. By gel filtration, it was demonstrated that SA affects the conformation of full-length NPRl , confirming the role of NPRI as an SA receptor. Gel filtration analysis also indicated that NPRI could be converted from an oligomer to a dimer with SA treatment. Furthermore, one N-terminal deletion ~513 has been shown to act as a metal-binding protein and its two Cys-521 and Cys-529 are important for binding to Ni 2 + by pull-down assays.