Parallel Architectures for Planetary Exploration Requirements (PAPER)

The Parallel Architectures for Planetary Exploration Requirements (PAPER) project is essentially research oriented towards technology insertion issues for NASA's unmanned planetary probes. It was initiated to complement and augment the long-term efforts for space exploration with particular reference to NASA/LaRC's (NASA Langley Research Center) research needs for planetary exploration missions of the mid and late 1990s. The requirements for space missions as given in the somewhat dated Advanced Information Processing Systems (AIPS) requirements document are contrasted with the new requirements from JPL/Caltech involving sensor data capture and scene analysis. It is shown that more stringent requirements have arisen as a result of technological advancements. Two possible architectures, the AIPS Proof of Concept (POC) configuration and the MAX Fault-tolerant dataflow multiprocessor, were evaluated. The main observation was that the AIPS design is biased towards fault tolerance and may not be an ideal architecture for planetary and deep space probes due to high cost and complexity. The MAX concepts appears to be a promising candidate, except that more detailed information is required. The feasibility for adding neural computation capability to this architecture needs to be studied. Key impact issues for architectural design of computing systems meant for planetary missions were also identified

Production of ferro Manganese Through Blast Furnace Route

High carbon ferro manganese is produced entirely through submerged arc furnace route in India. This route has the greatest disadvantage of high electrical energy consumption. The manufacturers of ferro alloys are facing difficulties to stay competitive due to the increasing tariff of electric power. Ferro manganese can be manufactured in blast furnaces much more economically compared to submerged arc furnaces with cogeneration of electric power using the BF off-gas. Some modifications will be required in the design of conventional blast furnaces for producing ferro manganese. Tana Kotf mini blast furnaces can be conveniently used for the manufacture of FeMn, since most of these modifications have already been incorporated in the design of these furnaces

Structural and mechanistic basis of anti-termination of Rho-dependent transcription termination by bacteriophage P4 capsid protein Psu

The conserved bacterial transcription terminator, Rho, is a potent target for bactericidal agents. Psu, a bacteriophage P4 capsid protein, is capable of inducing anti-termination to the Rho-dependent transcription termination. Knowledge of structural and mechanistic basis of this anti-termination is required to design peptide-inhibitor(s) of Rho from Psu. Using suppressor genetics, cross-linking, protein foot-printing and FRET analyses, we describe a conserved disordered structure, encompassing 139–153 amino acids of Rho, as the primary docking site for Psu. Also a neighbouring helical structure, comprising 347–354 amino acids, lining its central channel, plays a supportive role in the Rho–Psu complex formation. Based on the crystal structure of Psu, its conformation in the capsid of the P4 phage, and its interacting regions on Rho, we build an energy-minimized structural model of the Rho:Psu complex. In this model, a V-shaped dimer of Psu interacts with the two diagonally opposite subunits of a hexameric Rho, enabling Psu to form a ‘lid’ on the central channel of the latter. We show that this configuration of Psu makes the central channel of Rho inaccessible, and it causes a mechanical impediment to its translocase activity

NF-κB and the Immunoglobulin κ Gene Enhancer

Enhancers regulate lineage choice and the developmental timing of antigen receptor gene rearrangements. The transcription factor NF-κB has been implicated as a key component of the recombination and transcription activation potential of the immunoglobulin κ chain gene intronic enhancer. Here, I discuss the implications of the new observation that an NF-κB binding site–mutated enhancer in the correct biological context does not appear to affect κgene expression

N protein from lambdoid phages transforms NusA into an antiterminator by modulating NusA-RNA polymerase flap domain interactions

Interaction of the lambdoid phage N protein with the bacterial transcription elongation factor NusA is the key component in the process of transcription antitermination. A convex surface of E. coli NusA-NTD, located opposite to its RNA polymerase-binding domain (the β-flap domain), directly interacts with N in the antitermination complex. We hypothesized that this N-NusA interaction induces allosteric effects on the NusA-RNAP interaction leading to transformation of NusA into a facilitator of the antitermination process. Here we showed that mutations in β-flap domain specifically defective for N antitermination exhibited altered NusA-nascent RNA interaction and have widened RNA exit channel indicating an intricate role of flap domain in the antitermination. The presence of N reoriented the RNAP binding surface of NusA-NTD, which changed its interaction pattern with the flap domain. These changes caused significant spatial rearrangement of the β-flap as well as the β′ dock domains to form a more constricted RNA exit channel in the N-modified Elongation Complex (EC), which might play key role in converting NusA into a facilitator of the N antitermination. We propose that in addition to affecting the RNA exit channel and the active center of the EC, β-flap domain rearrangement is also a mechanistic component in the N antitermination process