Prof. Dr. Milena Bister

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Milena Bister erforscht die Schnittstellen zwischen medizinischer Praxis, Patientenhandeln und sozialen Strukturen – insbesondere in der psychiatrischen Versorgung und im Gesundheitswesen. Sie nutzt ethnographische Methoden, um zu verstehen, wie alltägliche Klassifizierungen, Dokumentationen und Entscheidungsprozesse die Gesundheitsversorgung und soziale Ungleichheit prägen. Ihre Expertise ist für Organisationen relevant, die Versorgungsprozesse, Patientenbeteiligung oder die Implementierung neuer Technologien in Gesundheitssystemen gestalten.

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Prof. Dr. Milena Bister

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Prof. Dr.

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Philosophische Fakultät

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Institut für Europäische Ethnologie

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Anthropologie von Mensch-Umwelt Beziehungen

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• Die Mobilisierung klinischer Versorgung: Eine qualitativ-ethnographische Pilotstudie zu den Versorgungspraktiken im psychatrischen Home Treatment

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  Förderer: DFG Eigene Stelle (Sachbeihilfe) Zeitraum: 01/2016 - 12/2017 Projektleitung: Prof. Dr. Milena Bister

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• Rio2p, an Evolutionarily Conserved, Low Abundant Protein Kinase Essential for Processing of 20 S Pre-rRNA in Saccharomyces cerevisiae

  2003

  Journal of Biological Chemistry · 83 Zitationen · DOI

  Saccharomyces cerevisiae Rio2p (encoded by open reading frame Ynl207w) is an essential protein of unknown function that displays significant sequence similarity to Rio1p/Rrp10p. The latter was recently shown to be an evolutionarily conserved, predominantly cytoplasmic serine/threonine kinase whose presence is required for the final cleavage at site D that converts 20 S pre-rRNA into mature 18 S rRNA. A data base search identified homologs of Rio2p in a wide variety of eukaryotes and Archaea. Detailed sequence comparison and in vitro kinase assays using recombinant protein demonstrated that Rio2p defines a subfamily of protein kinases related to, but both structurally and functionally distinct from, the one defined by Rio1p. Failure to deplete Rio2p in cells containing a GAL-rio2 gene and direct analysis of Rio2p levels by Western blotting indicated the protein to be low abundant. Using a GAL-rio2 gene carrying a point mutation that reduces the kinase activity, we found that depletion of this mutant protein blocked production of 18 S rRNA due to inhibition of the cleavage of cytoplasmic 20 S pre-rRNA at site D. Production of the large subunit rRNAs was not affected. Thus, Rio2p is the second protein kinase that is essential for cleavage at site D and the first in which the processing defect can be linked to its enzymatic activity. Contrary to Rio1p/Rrp10p, however, Rio2p appears to be localized predominantly in the nucleus. Saccharomyces cerevisiae Rio2p (encoded by open reading frame Ynl207w) is an essential protein of unknown function that displays significant sequence similarity to Rio1p/Rrp10p. The latter was recently shown to be an evolutionarily conserved, predominantly cytoplasmic serine/threonine kinase whose presence is required for the final cleavage at site D that converts 20 S pre-rRNA into mature 18 S rRNA. A data base search identified homologs of Rio2p in a wide variety of eukaryotes and Archaea. Detailed sequence comparison and in vitro kinase assays using recombinant protein demonstrated that Rio2p defines a subfamily of protein kinases related to, but both structurally and functionally distinct from, the one defined by Rio1p. Failure to deplete Rio2p in cells containing a GAL-rio2 gene and direct analysis of Rio2p levels by Western blotting indicated the protein to be low abundant. Using a GAL-rio2 gene carrying a point mutation that reduces the kinase activity, we found that depletion of this mutant protein blocked production of 18 S rRNA due to inhibition of the cleavage of cytoplasmic 20 S pre-rRNA at site D. Production of the large subunit rRNAs was not affected. Thus, Rio2p is the second protein kinase that is essential for cleavage at site D and the first in which the processing defect can be linked to its enzymatic activity. Contrary to Rio1p/Rrp10p, however, Rio2p appears to be localized predominantly in the nucleus. Like their counterparts in other eukaryotes, Saccharomyces cerevisiae ribosomes contain four species of rRNA: 5 S, 5.8 S, 18 S, and 25 S rRNAs. The genes encoding these rRNAs are organized on the yeast genome in 150–200 tandem repeats, each of which comprises two transcriptional units separated by non-transcribed spacers. One of these units consists of a 5 S rRNA gene, transcribed by RNA polymerase III. The other unit contains single genes for each of the mature 18 S, 5.8 S, and 25 S rRNAs that are separated by internal transcribed spacers 1 and 2, whereas external transcribed spacer regions are present at either end of the unit (see Fig. 1A). After transcription of this polycistronic unit by RNA polymerase I, the spacers are removed from the primary transcript via an ordered series of endo- and exonucleolytic cleavages (see Fig. 1B) (reviewed in Refs. 1Raué H.A. Olson M. The Nucleolus. Landes Bioscience, Georgetown, Washington, D. C.2003Google Scholar and 2Venema J. Tollervey D. Annu Rev. Genet. 1999; 33: 216-311Crossref Scopus (655) Google Scholar). The first detectable precursor species is 35 S pre-rRNA, which results from a cleavage at site B0 in the 3′-external transcribed spacer by the yeast RNase III homolog Rnt1p (3Abou-Elela S. Igel H. Ares Jr., M. Cell. 1996; 85: 115-124Abstract Full Text Full Text PDF PubMed Scopus (192) Google Scholar, 4Kufel J. Dichtl B. Tollervey D. RNA (N. Y.). 1999; 5: 909-917Crossref PubMed Scopus (125) Google Scholar). Subsequent cleavage at sites A0 and A1 in the 5′-external transcribed spacer first gives rise to 33 S and then 32 S pre-rRNA. The latter is cleaved at site A2 to produce separate 20 S and 27 S A2 precursors for the small and large ribosomal subunit, respectively. The majority (90%) of the 27 S A2 precursor molecules are cleaved endonucleolytically at site A3, followed by exonucleolytic trimming to B1S. The remainder are processed endonucleolytically 1A. W. Faber, J. C. Vos, and H. A. Raué, unpublished data. at site B1L. The resulting 27 S BS and 27 S BL precursors, whose 5′-ends are located 6 nucleotides apart, are then converted into 25 S rRNA and the “short” and “long” forms of 5.8 S rRNA, respectively, in the same manner (5Allmang C. Kufel J. Chanfreau G. Mitchell P. Petfalski E. Tollervey D. EMBO J. 1999; 18: 5399-5410Crossref PubMed Scopus (492) Google Scholar, 6Faber A.W. van Dijk M. Raué H.A. Vos J.C. RNA (N. Y.). 2002; 8: 1095-1101Crossref PubMed Scopus (44) Google Scholar, 7Mitchell P. Petfalski E. Tollervey D. Genes Dev. 1996; 10: 502-513Crossref PubMed Scopus (166) Google Scholar, 8Geerlings T. Vos J.C. Raué H.A. RNA (N. Y.). 2000; 6: 1698-1703Crossref PubMed Scopus (99) Google Scholar, 9Van Hoof A. Lennertz P. Parker R. EMBO J. 2000; PubMed Scopus Google Scholar). of the processing the of of the ribosomal in the the final in S subunit in yeast of the S ribosomal subunit to the its 20 S pre-rRNA is processed at site D to produce the mature 18 S rRNA Genes Dev. 1999; PubMed Scopus Google Scholar, E. C. J. M. EMBO J. PubMed Scopus Google Scholar). processing in other cells a that of 18 S rRNA is in the the the pre-rRNA processing is to its and its the of the ribosomal to be identified that are essential for in S. cerevisiae H.A. Olson M. The Nucleolus. Landes Bioscience, Georgetown, Washington, D. C.2003Google Scholar, A. Tollervey D. 2002; PubMed Scopus Google Scholar, D. P. J. Cell. 1999; PubMed Scopus Google Scholar). in the and of large the of that these two for the small and large A. Tollervey D. 2002; PubMed Scopus Google Scholar, Mitchell S. J. 2002; PubMed Scopus Google Scholar, P. J. Petfalski E. D. M. T. B. H. Tollervey D. E. Cell. 2002; 10: Full Text Full Text PDF PubMed Scopus Google Scholar, P. J. E. T. J. M. D. B. J. Jr., Cell. 8: Full Text Full Text PDF PubMed Scopus Google Scholar, J. Petfalski E. Tollervey D. E. EMBO J. 2002; PubMed Scopus Google Scholar). is the function of of the of these the manner in which of the to be in of the yeast S subunit are required for the of 20 S pre-rRNA by the processing cleavages at sites and on the pre-rRNA in the of the ribosomal to the S small subunit at for the to to of the S to the H.A. Olson M. The Nucleolus. Landes Bioscience, Georgetown, Washington, D. C.2003Google Scholar, A. Tollervey D. 2002; PubMed Scopus Google Scholar, Mitchell S. J. 2002; PubMed Scopus Google Scholar, P. J. Petfalski E. D. M. T. B. H. Tollervey D. E. Cell. 2002; 10: Full Text Full Text PDF PubMed Scopus Google Scholar). a of the S in the and to the T. D. Petfalski E. Tollervey D. E. EMBO J. PubMed Scopus Google Scholar). One of these is which is essential for the of 20 S pre-rRNA into mature 18 S rRNA and was identified in a a mutant of E. C. J. M. EMBO J. PubMed Scopus Google one of the of small M. W. J. Full Text Full Text PDF PubMed Scopus Google was shown to be a of a subfamily of serine/threonine protein kinases in eukaryotes, and A. 2002; PubMed Scopus Google Scholar, M. W. 2002; PubMed Scopus Google Scholar, M. A. W. 2002; PubMed Scopus Google Scholar). of in other in and that depletion of in yeast in the of the M. W. 2002; PubMed Scopus Google Scholar, M. A. W. 2002; PubMed Scopus Google Scholar). The these two of and its enzymatic the open reading frame a protein Rio2p that and similarity to Rio1p/Rrp10p. The function of Rio2p in yeast cells is but from that of both are A analysis of of yeast protein by G. A. B. M. M. B. 1999; PubMed Scopus Google demonstrated the of Rio2p on the one a of required in S and and on the other in and M. R. P. M. A. J. M. C. M. M. H. A. M. D. T. A. S. B. C. A. E. G. M. T. P. B. B. G. G. 2002; Scopus Google Scholar, A. A. A. P. C. S. J. M. J. M. B. C. D. H. H. A. E. J. J. T. D. M. D. M. 2002; PubMed Scopus Google Scholar). this we present that Rio2p is a of a second subfamily of protein kinases is essential for cleavage at site the final processing in the of mature 18 S rRNA. and yeast and in this are in and on yeast base containing the and either of cells in by at on a cerevisiae in this in a in this D. Tollervey D. 1996; PubMed Scopus Google P. PubMed Google from by of its and from by of the GAL-rio2 gene and to but containing mutation in of containing to but containing mutation in in a The for analysis was by first the carrying a gene by of the on one of its from the carrying a of the The resulting using the on the at that yeast base and and to for the presence of the After the on yeast and containing the gene identified by The containing the gene was The present in the cells was by the its mutant counterparts by of and Genes and of the gene the of its was by the gene of its sequence the and The resulting was the and sites of P. PubMed Google resulting in The gene was to the by first using the and The resulting was into D. Tollervey D. 1996; PubMed Scopus Google the and sites to the of in this either in of the in a (see Fig. into the by via the J. P. A using the and sites in the gene on the The for are in III. A tandem was by of the gene using the and The an site at the of the The was the and sites of a of PubMed Scopus Google that the and regions was into the and of the protein was by the of 1 to an After an at cells and by in containing 1 and The was for at in an to the to the resulting After for at the was in the same manner from cells a in which the by the mutant units of yeast cells in A and containing and at for The cells then by in an for 1 at in A containing and and at for The cells and in 5 and using a a The was at for 20 and then of a The resulting was separated into a cytoplasmic and a by for 20 at in an at RNA and RNA was by 20 units of cells in of and and of After of the at for 1 The was and of RNA was by of and of and in to a of analysis was using the indicated in Fig. J. Vos H. A.W. van Raué H.A. RNA (N. Y.). 2000; 6: PubMed Scopus Google Scholar). for Western blotting by the cells in 1 and 1 by for 5 The to on After blotting and the protein A was using and of recombinant by 5 of in 20 of containing 5 and 1 of either 5 the of Rio2p to a of protein was to the The by on a followed by The of present in the was by Rio2p a of a of S. cerevisiae open reading frame a Rio2p M. W. J. Full Text Full Text PDF PubMed Scopus Google that significant similarity to Rio1p/Rrp10p. The latter was found to be essential for cleavage at site the final in the of mature 18 S rRNA E. C. J. M. EMBO J. PubMed Scopus Google Scholar). was a predominantly cytoplasmic serine/threonine protein kinase from to a in A. 2002; PubMed Scopus Google Scholar, M. W. 2002; PubMed Scopus Google Scholar, M. A. W. 2002; PubMed Scopus Google Scholar). Fig. the results of an of and that the sequence the two are predominantly to regions indicated I, and III. is and III contain the and kinase M. A. W. 2002; PubMed Scopus Google Scholar). that Rio2p is a protein but to a subfamily distinct from the one defined by Rio1p/Rrp10p. Using the Rio2p sequence we the for homologs of Rio2p in other and identified a of homologs in both eukaryotes and Archaea. of these homologs a of sequence that is distinct from the one Rio2p and the regions of the but from the in which is not in the latter subfamily A. 2002; PubMed Scopus Google Scholar, M. A. W. 2002; PubMed Scopus Google Scholar). the regions that are and each of the two is the two these we that Rio2p defines a protein kinase subfamily that is related to, but distinct from, the one by Rio1p/Rrp10p. analysis to this analysis an and a small of to from a data base search not of the Rio2p Thus, whereas eukaryotes and at one gene in both the and the latter to be from the that the two of subfamily from of an gene that the and and Rio2p are both essential in the two genes of Rio2p to the of Rio2p in yeast in we a mutant that the the we the from contains a gene that by of the gene on one of its cells the carrying a gene the of its on and and on of an the of and analysis demonstrated that of the the gene, that is an essential gene A. H. B. R. R. H. C. M. E. G. T. M. H. A. M. P. M. C. C. P. B. M. S. S. M. G. R. P. M. 1999; PubMed Scopus Google Scholar). of cells carrying the in in four The resulting for to the presence of the gene for their to on to of the a final cells by to that the and the in which was found to the of depletion of we the which contains the gene the of the by and the of a from to on of the we found significant in the the for which we cells from of the that an the cells for on was Fig. not that the small of protein resulting from of the is to of in the by the for low of we to a of point at in the protein that either its activity. to located the the kinase site indicated in Fig. The mutant genes by (see and to the in the The resulting then into and on and and containing the to of the Rio2p cells for their to the by on containing and either the a single of the to on containing either that the Rio2p are and can transcription of the encoding gene is The was the mutant in which the at in the kinase to Rio2p containing the mutation to on not in the presence of that the mutation not the of the but this to an that low of the mutant gene is for the of the of the Rio2p either a not we the mutant to the function of Rio2p containing either was on and then to shown in Fig. the Rio2p a of the that low of Rio2p from the GAL-rio2 gene is to the of the to its to the of cells from both their to and a series of was on a in be the cells either the mutant that depletion of of the at is not to cells of M. A. W. 2002; PubMed Scopus Google cells containing the gene not on not Rio2p for of 20 S into 18 S Rio2p found to be in in the of S ribosomal M. R. P. M. A. J. M. C. M. M. H. A. M. D. T. A. S. B. C. A. E. G. M. T. P. B. B. G. G. 2002; Scopus Google we to the of depletion of on that RNA was from and cells at a from to The RNA to analysis using to the levels of the mature and precursor rRNA was on either 25 S 18 S rRNA production in the depletion of in a in the of 18 S rRNA the and the of 25 S rRNA a the mutant a of 20 S pre-rRNA in the of 32 S pre-rRNA. Thus, we that Rio2p a in S subunit either in the of the S in the final processing cleavage at site D. The in the of the 32 S precursor that the of Rio2p the cleavage at site not detectable for 25 S rRNA the of Rio2p in S subunit we the of the 20 S precursor in the cells using a from cells either the mutant gene on for by the followed by into a and a cytoplasmic using The of 20 S pre-rRNA in each of the was then by shown in Fig. cells containing the gene low of 20 S pre-rRNA in both 1 and in cells that the gene, a 20 S pre-rRNA was of which was present in the cytoplasmic and of cells a of 35 S and 27 S a small present in the cytoplasmic Thus, the of 20 S pre-rRNA found in the cytoplasmic from the mutant cells is not due to from in cells of the 20 S pre-rRNA from the but to be processed Rio2p a Rio2p is to function a protein kinase and the mutation this activity, we Rio2p to the in E. and from using (see the was on an in both a was at the of and and other was from the cells the same containing the gene a to but at the of we M. W. 2002; PubMed Scopus Google Scholar, M. A. W. 2002; PubMed Scopus Google is of by and in a followed by of the by Rio2p and to but the mutant protein was and in the that the kinase is due to the recombinant in this the mutant protein to be to and the of not the of not we the kinase of Rio2p and in the presence of 5 which shown to the of both and by M. W. 2002; PubMed Scopus Google Scholar). shown in Fig. the of not the of by Rio2p A and and in the presence of by Rio2p of the be The mutant protein was of these but this was to the same its results that Rio2p is a protein kinase and that the mutation its enzymatic activity. a we other Rio2p Fig. and the results for the mutant in which which is in both the Rio2p and was into both the and of Rio2p at by this the that the of Rio2p in pre-rRNA processing is linked to its enzymatic activity. to the kinase of the mutation in the kinase we to this mutant protein in E. the of a detectable defect depletion of the this not the enzymatic activity. Rio2p at a and the of we from which contains a gene by its that a of the to using not due to the low of the protein (see to protein was from both the and cytoplasmic from cells and separated on a Rio2p was then by Western blotting using an the of the a we the same a protein to be localized to the H. M. Tollervey D. B. EMBO J. PubMed Scopus Google Scholar, C. M. T. EMBO J. PubMed Scopus Google Scholar). shown in Fig. be and was found predominantly in the was of the cytoplasmic of the and cytoplasmic from containing the same of protein produce a for in the however, was that for Rio2p was detectable in the cytoplasmic not these we that Rio2p is a predominantly protein and that the of Rio2p from its is at of that of The latter is in to deplete Rio2p the required for in cells containing a GAL-rio2 gene a from to the and identified essential for the of ribosomes in the yeast S. cerevisiae J. Tollervey D. Annu Rev. Genet. 1999; 33: 216-311Crossref Scopus (655) Google Scholar, D. P. J. Cell. 1999; PubMed Scopus Google Scholar). The majority homologs in other from to the of the of that these are of two that on the pre-rRNA and its processing and ordered the ribosomal into the small and large H.A. Olson M. The Nucleolus. Landes Bioscience, Georgetown, Washington, D. C.2003Google Scholar, A. Tollervey D. 2002; PubMed Scopus Google Scholar, Mitchell S. J. 2002; PubMed Scopus Google Scholar, P. J. Petfalski E. D. M. T. B. H. Tollervey D. E. Cell. 2002; 10: Full Text Full Text PDF PubMed Scopus Google Scholar, J. Petfalski E. Tollervey D. E. EMBO J. 2002; PubMed Scopus Google Scholar). of these is in its from the and required for the of the spacer are to RNA and ribosomal protein and in and (reviewed in Refs. 1Raué H.A. Olson M. The Nucleolus. Landes Bioscience, Georgetown, Washington, D. C.2003Google Scholar, A. Tollervey D. 2002; PubMed Scopus Google Scholar, D. P. J. Cell. 1999; PubMed Scopus Google Scholar, and J. Petfalski E. Tollervey D. E. EMBO J. 2002; PubMed Scopus Google Scholar). protein kinases to this by the that Rio1p/Rrp10p, a predominantly cytoplasmic serine/threonine protein kinase M. W. 2002; PubMed Scopus Google Scholar, M. A. W. 2002; PubMed Scopus Google is essential for the cleavage of 20 S pre-rRNA at site D that mature 18 S rRNA E. C. J. M. EMBO J. PubMed Scopus Google Scholar). The data in this a second protein required for this final in 18 S rRNA and a its enzymatic and 20 S pre-rRNA Rio2p significant sequence similarity to in contains the in and kinase comparison indicated that the two to separate and by is the of this subfamily are found in A. 2002; PubMed Scopus Google whereas of the Rio2p subfamily are data base search identified in species that from both and but a subfamily and Rio2p both genes are essential and M. A. W. 2002; PubMed Scopus Google Scholar). analysis Cell. Full Text Full Text PDF PubMed Scopus Google indicated that both are at low levels of data that the for Rio2p is that for Rio1p/Rrp10p. the latter protein is functionally by transcription of a gene E. C. J. M. EMBO J. PubMed Scopus Google Scholar, M. A. W. 2002; PubMed Scopus Google GAL-rio2 cells at on both and containing Fig. the of the production of Rio2p to The Western shown in Fig. the that Rio2p is a low at a that of the small The of a detectable in cells the of a Rio2p that we in the and kinase in the of a gene of the to on into a both a and a at in the of either in the and of in the kinase Thus, of these which are in Rio1p/Rrp10p, are essential for the function of the a of a whereas the mutant protein to on a to a in the the demonstrated a in the of 18 S rRNA, whereas production of the large subunit rRNAs The of 18 S rRNA is due to a in cleavage of its precursor at site D inhibition of of S 20 S pre-rRNA predominantly in the Thus, Rio1p/Rrp10p, Rio2p is required for the final cytoplasmic processing in 18 S rRNA but at a the other of a that be functionally from a gene is a required for the in of 5.8 S rRNA A.W. van Dijk M. Raué H.A. Vos J.C. RNA (N. Y.). 2002; 8: 1095-1101Crossref PubMed Scopus (44) Google Scholar). to the of Rio2p in cytoplasmic processing of 20 S pre-rRNA, indicated that the protein is predominantly located in the is in the presence of Rio2p in a containing a of and M. R. P. M. A. J. M. C. M. M. H. A. M. D. T. A. S. B. C. A. E. G. M. T. P. B. B. G. G. 2002; Scopus Google which are predominantly in S subunit A. Tollervey D. 2002; PubMed Scopus Google Scholar, D. J. J. J. J. PubMed Scopus Google Scholar, D. J. J. RNA (N. Y.). PubMed Scopus Google Scholar). is of both the and cytoplasmic S subunit D. J. J. J. J. PubMed Scopus Google Scholar, D. J. Tollervey D. Genes Dev. PubMed Scopus Google and the other of the to the S its from the A. Tollervey D. 2002; PubMed Scopus Google Scholar, T. D. Petfalski E. Tollervey D. E. EMBO J. PubMed Scopus Google Scholar). A the of Rio2p for cytoplasmic processing of 20 S pre-rRNA its for of Rio2p was this was T. D. Petfalski E. Tollervey D. E. EMBO J. PubMed Scopus Google Scholar, E. M. Cell. PubMed Scopus Google Scholar). the low for Rio2p that a of the S The in vitro assays using recombinant protein demonstrated that Rio2p is a protein kinase of both and the latter required the of in the The significant in both and by the mutation a the enzymatic of Rio2p and its in 20 S pre-rRNA is by the that the mutation in the kinase of Rio2p not the kinase activity. the that the processing of the mutant is due to a of the mutant protein a kinase activity. be the of a of of the mutant protein to its this to be mutation of the not the of Rio2p to from a that this mutant is at a The of Rio2p in and and and M. R. P. M. A. J. M. C. M. M. H. A. M. D. T. A. S. B. C. A. E. G. M. T. P. B. B. G. G. 2002; Scopus Google Scholar, A. A. A. P. C. S. J. M. J. M. B. C. D. H. H. A. E. J. J. T. D. M. D. M. 2002; PubMed Scopus Google Scholar, T. T. R. M. M. S. A. PubMed Scopus Google that Rio2p is a protein a in both and of to that not a the cells not of at a of the in to the analysis of which indicated either into S from M. A. W. 2002; PubMed Scopus Google Scholar). the of the mutation in Rio2p on both its enzymatic and 20 S pre-rRNA processing a its enzymatic and its in cleavage of 20 S pre-rRNA at site the of Rio2p the of the pre-rRNA processing defect be a a The of Rio2p the in the of S subunit T. D. Petfalski E. Tollervey D. E. EMBO J. PubMed Scopus Google Scholar, M. R. P. M. A. J. M. C. M. M. H. A. M. D. T. A. S. B. C. A. E. G. M. T. P. B. B. G. G. 2002; Scopus Google in of the The of this enzymatic Rio2p of the S to be of of the small subunit not demonstrated was found to 20 S pre-rRNA, that is the S and E. C. J. M. EMBO J. PubMed Scopus Google Scholar). The of that its kinase and M. A. W. 2002; PubMed Scopus Google on 20 S pre-rRNA processing to be are for that function in both and pre-rRNA is required for exonucleolytic processing of 27 S pre-rRNA, whereas mutant of the gene depletion of the protein in G. J. P. J. Full Text Full Text PDF PubMed Scopus Google Scholar, B. Cell. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar, M. A. Tollervey D. RNA (N. Y.). 2002; 8: PubMed Scopus Google Scholar). A function for its homolog A. J. J. G. P. J. 2002; Full Text Full Text PDF PubMed Scopus (99) Google Scholar). is required for cleavage at site internal transcribed spacer PubMed Scopus Google and a of which a inhibition of pre-rRNA processing a J. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). A is which is in S subunit P. J. E. T. J. M. D. B. J. Jr., Cell. 8: Full Text Full Text PDF PubMed Scopus Google and is essential for 1999; PubMed Scopus (192) Google Scholar). are found in S A. Tollervey D. 2002; PubMed Scopus Google in in of the of and B. Cell. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). Thus, are for and S that and Rio2p a at the of S subunit for and reading of the van for in the of the point in and for the of this

• Refusing the information paradigm: informed consent, medical research, and patient participation

  2008

  Health An Interdisciplinary Journal for the Social Study of Health Illness and Medicine · 80 Zitationen · DOI

  This article challenges the assumption that patient autonomy can best be assured by providing proper information through formalized procedures such as informed consent. We suggest that to understand and consider laypeople's ways of knowing and decision making, one has to move beyond the information paradigm and take into account a much broader context. Concretely, we investigate informed consent in connection with donating skin tissue remaining from medically indicated surgery. We use interviews with patients and observation protocols to analyse patients' perceptions and ways of making sense of informed consent beyond its bioethical ideal. Patients situate themselves in a larger system of solidarity, enroll in an overall positive image of science as a linear process of innovation oriented towards output, and simultaneously take a pragmatic stance towards hospital routines as a necessary passage point towards receiving good treatment. Because informed consent is one of the central articulations between the biomedical system and society, we conclude by reflecting on the consequences of our findings on a socio-political level.

• Distributing Reflexivity through Co-laborative Ethnography

  2020

  Journal of Contemporary Ethnography · 68 Zitationen · DOI

  In ethnographic research and analysis, reflexivity is vital to achieving constant coordination between field and concept work. However, it has been conceptualized predominantly as an ethnographer’s individual mental capacity. In this article, we draw on ten years of experience in conducting research together with partners from social psychiatry and mental health care across different research projects. We unfold three modes of achieving reflexivity co-laboratively: contrasting and discussing disciplinary concepts in interdisciplinary working groups and feedback workshops; joint data interpretation and writing; and participating in political agenda setting. Engaging these modes reveals reflexivity as a distributed process able to strengthen the ethnographer’s interpretative authority, and also able to constantly push the conceptual boundaries of the participating disciplines and professions.

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