156,802 research outputs found
Austronesian and the Vocabulary of Languages of the Reef and Santa Cruz Islands - a preliminary approach
W. C. Mccormack & S. A. Wurm, eds., Language and Man. Anthropological Issues
Legrand-Gelber Régine. W. C. Mccormack & S. A. Wurm, eds., Language and Man. Anthropological Issues. In: L'Homme, 1978, tome 18 n°1-2. pp. 231-233
Is "Addiction" a helpful concept? An existential view
This paper was originally published in “Psychotherapy in Australia” volume 7, number 2 in February 2001 and appears here by kind permission of the publishers.Ideas about addiction have evolved, and today behaviours such as excessive gambling and sex are called addictions. Medication and psychotherapy are offered, but many people avoid treatment. The dominant “bio-psycho-social model”, despite being holistic, does not address freedom, motivation or spirituality, and some common terms and ways of working offend or alienate drug-takers, indirectly perpetuating their problems. Here CHRISTOPHER WURM argues for a reconsideration of the concept of “addiction”.Christopher Wur
W. C. Mccormack & S. A. Wurm, eds., Language and Man. Anthropological Issues
Legrand-Gelber Régine. W. C. Mccormack & S. A. Wurm, eds., Language and Man. Anthropological Issues. In: L'Homme, 1978, tome 18 n°1-2. pp. 231-233
Rapid FlAsH labelling in the budding yeast Saccharomyces cerevisiae.
P>Live cell imaging of protein distributions is an essential tool in modern cell biology. It relies on the functional labelling of a host protein with a fluorophore, which may either be a genetically fused fluorescent protein or an organic dye binding to the host protein. The biarsenical-tetracysteine system or 'FlAsH-labelling', is based on the high affinity interaction between a biarsenical probe and a small protein tag. This approach has been successfully used for live cell imaging in the budding yeast Saccharomyces cerevisiae. However, the established labelling protocols require a lengthy overnight incubation of the cells with the dye under tightly controlled growth conditions, which severely limits the use of this approach. In this study, we characterize an efficient method for introducing FlAsH-EDT(2) into live budding yeast cells using standard electroporation. The labelling time is reduced from more than 12 h to less than 1 h without compromising the labelling efficiency or cell viability. This approach may be used for cells in different growth phases or grown under different conditions. It may be further extended to other small high affinity probes, thus opening up new possibilities for labelling in budding yeast
The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria.
The m-AAA protease is a conserved hetero-oligomeric complex in the inner membrane of mitochondria. Recent evidence suggests a compartmentalization of the contiguous mitochondrial inner membrane into an inner boundary membrane (IBM) and a cristae membrane (CM). However, little is known about the functional differences of these subdomains. We have analyzed the localizations of the m-AAA protease and its substrate cytochrome c peroxidase (Ccp1) within yeast mitochondria using live cell fluorescence microscopy and quantitative immunoelectron microscopy. We find that the m-AAA protease is preferentially localized in the IBM. Likewise, the membrane-anchored precursor form of Ccp1 accumulates in the IBM of mitochondria lacking a functional m-AAA protease. Only upon proteolytic cleavage the mature form mCcp1 moves into the cristae space. These findings suggest that protein quality control and proteolytic activation exerted by the m-AAA protease take place preferentially in the IBM pointing to significant functional differences between the IBM and the CM
Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
AbstractThe mitochondrial inner membrane exhibits a complex topology. Its infolds, the cristae membranes, are contiguous with the inner boundary membrane (IBM), which runs parallel to the outer membrane. Using live cells co-expressing functional fluorescent fusion proteins, we report on the distribution of inner membrane proteins in budding yeast. To this end we introduce the enlarged mitochondria of Δmdm10, Δmdm31, Δmdm32, and Δmmm1 cells as a versatile model system to study sub-mitochondrial protein localizations. Proteins of the F1F0 ATP synthase and of the respiratory chain complexes III and IV were visualized in the cristae-containing interior of the mitochondria. In contrast, proteins of the TIM23 complex and of the presequence translocase-associated motor were strongly enriched at the IBM. The different protein distributions shown here demonstrate that the cristae membranes and the IBM are functionally distinct sub-compartments
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