Distributed Network Protocol (DNP3) is the predominant SCADA protocol in the energy sector-more than 75% of North American electric utilities currently use DNP3 for industrial control applications. This paper presents a taxonomy of attacks on the protocol. The attacks are classified based on targets (control center, outstation devices and network/communication paths) and threat categories (interception, interruption, modification and fabrication). To facilitate risk analysis and mitigation strategies, the attacks are associated with the specific DNP3 protocol layers they exploit. Also, the operational impact of the attacks is categorized in terms of three key SCADA objectives: process confidentiality, process awareness and process control. The attack taxonomy clarifies the nature and scope of the threats to DNP3 systems, and can provide insights into the relative costs and benefits of implementing mitigation strategies.
Group VII ethylene response factors (ERF-VIIs) regulate transcriptional adaptation to flooding-induced hypoxia in plants. ERF-VII stability is controlled in an O2-dependent manner by the Cys/Arg branch of the N-end rule pathway whereby oxidation of a conserved N-terminal cysteine residue initiates target degradation. This oxidation is catalyzed by plant cysteine oxidases (PCOs), which use O2 as cosubstrate to generate Cys-sulfinic acid. The PCOs directly link O2 availability to ERF-VII stability and anaerobic adaptation, leading to the suggestion that they act as plant O2 sensors. However, their ability to respond to fluctuations in O2 concentration has not been established. Here, we investigated the steady-state kinetics of Arabidopsis thaliana PCOs 1–5 to ascertain whether their activities are sensitive to O2 levels. We found that the most catalytically competent isoform is AtPCO4, both in terms of responding to O2 and oxidizing AtRAP2.2/2,12 (two of the most prominent ERF-VIIs responsible for promoting the hypoxic response), which suggests that AtPCO4 plays a central role in ERF-VII regulation. Furthermore, we found that AtPCO activity is susceptible to decreases in pH and that the hypoxia-inducible AtPCOs 1/2 and the noninducible AtPCOs 4/5 have discrete AtERF-VII substrate preferences. Pertinently, the AtPCOs had Km(O2)app values in a physiologically relevant range, which should enable them to sensitively react to changes in O2 availability. This work validates an O2-sensing role for the PCOs and suggests that differences in expression pattern, ERF-VII selectivity, and catalytic capability may enable the different isoforms to have distinct biological functions. Individual PCOs could therefore be targeted to manipulate ERF-VII levels and improve stress tolerance in plants.
The centromere is a unique chromatin domain that links sister chromatids and forms the attachment site for spindle microtubules in mitosis. Centromere inheritance is largely DNA sequence-independent but strongly reliant on a self-propagating chromatin domain featuring nucleosomes containing the H3 variant CENP-A. Unlike other histones, CENP-A is maintained with unusually high stability in chromatin. Previously, we have shown that mitotic maintenance of CENP-A and other CCAN proteins is controlled by a dynamic SUMO cycle and that the deSUMOylase SENP6 is necessary for stable maintenance of CENP-A at the centromere. Here, we discover that the removal of SENP6 leads to a rapid loss of the constitutive centromere-associated network (CCAN), followed by a delayed loss of centromeric CENP-A, indicating that the CCAN is the primary SUMO target. We found the ATP-dependent segregase p97/VCP removes centromeric CENP-A in a SUMO-dependent manner and physically interacts with the CCAN and CENP-A chromatin. Our data suggest a direct role of p97 in removing centromeric CENP-A via SUMOylated CCAN proteins thereby ensuring centromere homeostasis and potentially preventing ectopic CENP-A accumulation.
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