92 research outputs found

    Regulating the Energy Flow in a Cyanobacterial Light Harvesting Antenna Complex

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    Photosynthetic organisms harvest light energy, utilizing the absorption and energy transfer properties of protein-bound chromophores. Controlling the harvesting efficiency is critical for the optimal function of the photosynthetic apparatus. Here, we show that cyanobacterial light-harvesting antenna may be able to regulate the flow of energy in order to switch reversibly from efficient energy conversion to photo-protective quenching via a structural change. We isolated cyanobacterial light harvesting proteins, phycocyanin and allophycocyanin, and measured their optical properties in solution and in an aggregated-desiccated state. The results indicate that energy band structures are changed, generating a switch between two modes of operation: exciton transfer and quenching; achieved without dedicated carotenoid quenchers. This flexibility can contribute greatly to the large dynamic range of cyanobacterial light harvesting systems.Comment: Published at J. Phys. Chem.

    Linking the Five-Factors of personality to charismatic and transactional leadership; Perceived dynamic work environment as a moderator

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    In this multi-source study we investigated the relationships between the Big Five personality traits and both charismatic and transactional leadership behavior, and whether dynamism (the degree that the work environment is deemed dynamic) moderates these relationships. We also tested whether dynamism moderates the relationship between leadership behavior and effectiveness. Personality was measured through self ratings using the NEO-PI-R. Subordinates rated their leaders' behavior, and peers and superiors provided ratings of effectiveness. Consistent with trait activation theory, results showed that perceived dynamic work environment moderated the relationships of four of the Big Five-Factors with both charismatic and transactional leadership. Also, charismatic leadership was positively related to perceived effectiveness, but only in dynamic contexts. Copyright © 2005 John Wiley & Sons, Ltd

    Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats.

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    Broken chromosomes arising from DNA double-strand breaks result from endogenous events such as the production of reactive oxygen species during cellular metabolism, as well as from exogenous sources such as ionizing radiation. Left unrepaired or incorrectly repaired they can lead to genomic changes that may result in cell death or cancer. DNA-dependent protein kinase (DNA-PK), a holoenzyme that comprises the DNA-PK catalytic subunit (DNA-PKcs) and the heterodimer Ku70/Ku80, has a major role in non-homologous end joining-the main pathway in mammals used to repair double-strand breaks. DNA-PKcs is a serine/threonine protein kinase comprising a single polypeptide chain of 4,128 amino acids and belonging to the phosphatidylinositol-3-OH kinase (PI(3)K)-related protein family. DNA-PKcs is involved in the sensing and transmission of DNA damage signals to proteins such as p53, setting off events that lead to cell cycle arrest. It phosphorylates a wide range of substrates in vitro, including Ku70/Ku80, which is translocated along DNA. Here we present the crystal structure of human DNA-PKcs at 6.6 A resolution, in which the overall fold is clearly visible, to our knowledge, for the first time. The many alpha-helical HEAT repeats (helix-turn-helix motifs) facilitate bending and allow the polypeptide chain to fold into a hollow circular structure. The carboxy-terminal kinase domain is located on top of this structure, and a small HEAT repeat domain that probably binds DNA is inside. The structure provides a flexible cradle to promote DNA double-strand-break repair

    Conceptualizing leadership perceptions as attitudes:using attitude theory to further the understanding of the relation between leadership and outcomes

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    Leadership is one of the most examined factors in relation to understanding employee wellbeing and performance. While there are disparate approaches to studying leadership, they share a common assumption that perceptions of a leader's behavior determine reactions to the leader. The concept of leadership perception is poorly understood in most theoretical approaches. To address this, we propose that there are many benefits from examining leadership perceptions as an attitude towards the leader. In this review, we show how research examining a number of aspects of attitudes (content, structure and function) can advance understanding of leadership perceptions and how these affect work-related outcomes. Such a perspective provides a more multi-faceted understanding of leadership perceptions than previously envisaged and this can provide a more detailed understanding of how such perceptions affect outcomes. In addition, we examine some of the main theoretical and methodological implications of viewing leadership perceptions as attitudes to the wider leadership area. The cross-fertilization of research from the attitudes literature to understanding leadership perceptions provides new insights into leadership processes and potential avenues for further research. (C) 2015 Elsevier Inc. All rights reserve

    A NOTE ON RICH LINES IN TRULY HIGH DIMENSIONAL SETS

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    Orange carotenoid protein burrows into the phycobilisome to provide photoprotection.

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    International audienceIn cyanobacteria, photoprotection from overexcitation of photochemical centers can be obtained by excitation energy dissipation at the level of the phycobilisome (PBS), the cyanobacterial antenna, induced by the orange carotenoid protein (OCP). A single photoactivated OCP bound to the core of the PBS affords almost total energy dissipation. The precise mechanism of OCP energy dissipation is yet to be fully determined, and one question is how the carotenoid can approach any core phycocyanobilin chromophore at a distance that can promote efficient energy quenching. We have performed intersubunit cross-linking using glutaraldehyde of the OCP and PBS followed by liquid chromatography coupled to tandem mass spectrometry (LC/MS-MS) to identify cross-linked residues. The only residues of the OCP that cross-link with the PBS are situated in the linker region, between the N- and C-terminal domains and a single C-terminal residue. These links have enabled us to construct a model of the site of OCP binding that differs from previous models. We suggest that the N-terminal domain of the OCP burrows tightly into the PBS while leaving the OCP C-terminal domain on the exterior of the complex. Further analysis shows that the position of the small core linker protein ApcC is shifted within the cylinder cavity, serving to stabilize the interaction between the OCP and the PBS. This is confirmed by a ΔApcC mutant. Penetration of the N-terminal domain can bring the OCP carotenoid to within 5-10 Å of core chromophores; however, alteration of the core structure may be the actual source of energy dissipation
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