The Evaluation of Concentrations Under the Merger Control Regulation: The Nature of the Beast

Part I of this Article examines whether, in evaluating a concentration, the Commission of the European Communities is permitted to take into account factors, such as industrial or social policy, that are not, strictly speaking, related to competition law. Part II explores whether “dominant position” has the same meaning under the Regulation No. 4064/89 as under Article 86 of the Treaty Establishing the European Economic Community and, in particular, whether the Regulation also applies to concentrations that create, or further narrow, interdependent oligopolies. Part III examines whether the Commission is required to prohibit or modify every concentration that creates or strengthens a dominant position, or whether it is required to do so only when a further evaluation indicates that the concentration will result in effective competition being substantially impeded in all or a substantial part of the common market. The Article concludes with some reflections on market definitions, customer dependence and vertical concentrations

The Power of Peer Pressure: Incorporating Social Comparison Into Traditional Anti-Food Waste Campaigns and its Potential Effects on College Campuses

Food waste is a major contributor to climate change, one of the most pressing environmental challenges of our time. Addressing this problem would not only protect the environment, but it would also save trillions of dollars and help to reduce the staggering number of people in the world today who are chronically malnourished. This paper focuses on the potential of using behavioral economic theory, particularly the concept of “nudging” in addressing the problem of food waste. Existing literature on nudges and food waste mainly focuses on how feedback and manipulating plate size can reduce food waste. Another proven approach to “nudging” is the use of social influence. Thus, my proposed experiment will investigate the question: could incorporating social comparisons into traditional anti-food waste feedback campaigns have a significant effect on the amount of food waste, particularly in university dining halls? The study will take place in the four “all-you-care-to-eat” dining halls at Penn. The participants will be students who are enrolled in a university meal plan and choose to eat at those dining halls during the five week period in which this experiment will take place. Materials will include separate food waste only trash bins for each of the dining halls, scales to measure the food waste, a device to count how many students eat at the dining hall each day, preliminary and post-experiment surveys, and posters for each of the four treatment conditions. Expected results are based on existing literature in behavioral economics and psychology

Isoformy proteínu myosin 1c a jejich funkce v buněčném jádře a v cytoplasmě

Nuclear myosin 1 (NM1) was the first myosin described in the cell nucleus. From its discovery, it has been found to function in processes of Pol I and Pol II transcription, chromatin remodeling, and chromosomal movements. However, direct mechanisms of how NM1 works in the cell nucleus were still missing. We therefore decided to prepare NM1 knock-out mice to answer questions about phyiological functioning of this protein. Myo1c is an isoform of NM1 protein, previously described in the cytoplasm. The only difference between these isoforms is 16 amino-acids at the N-terminus of NM1, which were thought to be the nuclear localization signal. However, we discovered that the nuclear localization signal is located in the neck domain of myosin, and therefore it is able to direct both isoforms to the nucleus. Moreover, we found that the ratio between both proteins is nearly the same in the nucleus and deletion of NM1 does not cause compensatory overexpression of Myo1c. NM1 KO mice are fully viable with minor changes in bone mineral density and red blood cells size. We found that the function of NM1 in processes such as Pol I transcription can be fully covered by Myo1c protein, suggesting redundancy and interchangeability of these two isoforms in the cell nucleus. We also found that PIP2, a phosphoinositol...Souhrn Jaderný myosin 1 je první myosin, který byl nalezený v buněčném jádře. Účastní se procesů jako je transkripce polymerasami I a II, remodelace chromatinu a pohyby chromosomů. Dosud však nebyl popsán přesný mechanismus funkce NM1 v buněčném jádře. Proto jsme připravili myš, která má deleci v genu kódujícím NM1 (NM1 KO). Myo1c je izoforma NM1, která byla charakterizována jako cytoplasmatická. Jediným rozdílem mezi těmito dvěma izoformami je 16 aminokyselin, které obsahuje NM1 na svém N-konci a které byly dříve považovány za jaderný lokalizační signál. Nám se ale podařilo ukázat, že obě izoformy jsou translokovány do jádra, protože jaderný lokalizační signál se nachází v krku, což je doména, která je společná pro obě izoformy. Navíc jsme ukázali, že poměr mezi oběma izoformami je v jádře i v cytoplasmě stejný a delece NM1 nezpůsobuje kompenzační expresi Myo1c. NM1 KO myši jsou životaschopné a vykazují minoritní změny v minerální hustotě kostí a velikosti červených krvinek. Dále jsme zjistili, že Myo1c může NM1 zastoupit ve funkcích jako je transkripce polymerasou I, což naznačuje, že tyto dvě izoformy jsou v buněčném jádře zaměnitelné a duplicitní. V cytoplasmě byla popsána interakce mezi Myo1c a PIP2, lipidem ze skupiny fosfoinositolů. Ukázali jsme, že PIP2 se nachází i v jádře, kde přispívá k propojení...Department of Cell BiologyKatedra buněčné biologieFaculty of SciencePřírodovědecká fakult

Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus.

Nuclear myosin I (NM1) is a nuclear isoform of the well-known "cytoplasmic" Myosin 1c protein (Myo1c). Located on the 11(th) chromosome in mice, NM1 results from an alternative start of transcription of the Myo1c gene adding an extra 16 amino acids at the N-terminus. Previous studies revealed its roles in RNA Polymerase I and RNA Polymerase II transcription, chromatin remodeling, and chromosomal movements. Its nuclear localization signal is localized in the middle of the molecule and therefore directs both Myosin 1c isoforms to the nucleus. In order to trace specific functions of the NM1 isoform, we generated mice lacking the NM1 start codon without affecting the cytoplasmic Myo1c protein. Mutant mice were analyzed in a comprehensive phenotypic screen in cooperation with the German Mouse Clinic. Strikingly, no obvious phenotype related to previously described functions has been observed. However, we found minor changes in bone mineral density and the number and size of red blood cells in knock-out mice, which are most probably not related to previously described functions of NM1 in the nucleus. In Myo1c/NM1 depleted U2OS cells, the level of Pol I transcription was restored by overexpression of shRNA-resistant mouse Myo1c. Moreover, we found Myo1c interacting with Pol II. The ratio between Myo1c and NM1 proteins were similar in the nucleus and deletion of NM1 did not cause any compensatory overexpression of Myo1c protein. We observed that Myo1c can replace NM1 in its nuclear functions. Amount of both proteins is nearly equal and NM1 knock-out does not cause any compensatory overexpression of Myo1c. We therefore suggest that both isoforms can substitute each other in nuclear processes

The Maya wall paintings from Chajul, Guatemala

The recent renovation of a house in Chajul in western Guatemala has revealed an unparalleled set of wall paintings, most probably from the Colonial period (AD 1524-1821). The iconography of the murals combines pre-Columbian elements with imported European components in a domestic rather than a religious setting, making them a unique example of Colonial-period art. Here, the authors present the results of iconographic, chemical and radiocarbon analyses of the Chajul house paintings. Dating to the seventeenth to eighteenth centuries AD, the paintings may be connected to a revival of the local religious organisations (cofradías) in the context of waning Spanish colonial control

Specific Nuclear Localizing Sequence Directs Two Myosin Isoforms to the Cell Nucleus in Calmodulin-Sensitive Manner

BACKGROUND: Nuclear myosin I (NM1) was the first molecular motor identified in the cell nucleus. Together with nuclear actin, they participate in crucial nuclear events such as transcription, chromatin movements, and chromatin remodeling. NM1 is an isoform of myosin 1c (Myo1c) that was identified earlier and is known to act in the cytoplasm. NM1 differs from the "cytoplasmic" myosin 1c only by additional 16 amino acids at the N-terminus of the molecule. This amino acid stretch was therefore suggested to direct NM1 into the nucleus. METHODOLOGY/PRINCIPAL FINDINGS: We investigated the mechanism of nuclear import of NM1 in detail. Using over-expressed GFP chimeras encoding for truncated NM1 mutants, we identified a specific sequence that is necessary for its import to the nucleus. This novel nuclear localization sequence is placed within calmodulin-binding motif of NM1, thus it is present also in the Myo1c. We confirmed the presence of both isoforms in the nucleus by transfection of tagged NM1 and Myo1c constructs into cultured cells, and also by showing the presence of the endogenous Myo1c in purified nuclei of cells derived from knock-out mice lacking NM1. Using pull-down and co-immunoprecipitation assays we identified importin beta, importin 5 and importin 7 as nuclear transport receptors that bind NM1. Since the NLS sequence of NM1 lies within the region that also binds calmodulin we tested the influence of calmodulin on the localization of NM1. The presence of elevated levels of calmodulin interfered with nuclear localization of tagged NM1. CONCLUSIONS/SIGNIFICANCE: We have shown that the novel specific NLS brings to the cell nucleus not only the "nuclear" isoform of myosin I (NM1 protein) but also its "cytoplasmic" isoform (Myo1c protein). This opens a new field for exploring functions of this molecular motor in nuclear processes, and for exploring the signals between cytoplasm and the nucleus

Myosin VI regulates the spatial organisation of mammalian transcription initiation.

During transcription, RNA Polymerase II (RNAPII) is spatially organised within the nucleus into clusters that correlate with transcription activity. While this is a hallmark of genome regulation in mammalian cells, the mechanisms concerning the assembly, organisation and stability remain unknown. Here, we have used combination of single molecule imaging and genomic approaches to explore the role of nuclear myosin VI (MVI) in the nanoscale organisation of RNAPII. We reveal that MVI in the nucleus acts as the molecular anchor that holds RNAPII in high density clusters. Perturbation of MVI leads to the disruption of RNAPII localisation, chromatin organisation and subsequently a decrease in gene expression. Overall, we uncover the fundamental role of MVI in the spatial regulation of gene expression