5711
1994
eng
article
1
2012-03-19
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Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy
Cytokines are hormones that carry information from ceJI to ceH. This information is read from their surface upon binding to transmembrane receptors and by the subsequent initiation of receptor oligomerization. An inftuence on this process through mutagenesis on the hormone surface is highly desirab)e for medical reasons. However, an understanding of hormone-receptor interactions requires insight into the structural changes introduced by the mutations. In this line structural studies on human TL-4 and the medically important IL-4 antagonists YI24D and Y124G are presented. The site a.round YI24 is an important epitope responsible for the a.bility of 11-4 t.o ca.use a signal in the target cells. It is shown that the local main-chain structure around residue 124 in the variants remains unchanged. A strategy is presented here which allows the study of these types of proteins and their variants by NMR which does not require carbon Iabeiied sa.mples.
urn:nbn:de:bvb:20-opus-62444
6244
In: Journal of molecular biology (1994 Apr) 4, 237, 423-436.
Deutsches Urheberrecht
T. Müller
T. Dieckmann
Walter Sebald
H. Oschkinat
deu
swd
Biochemie
eng
uncontrolled
Interleukin-4
eng
uncontrolled
protein structure
eng
uncontrolled
NMR
eng
uncontrolled
signal transduction
Biowissenschaften; Biologie
open_access
Theodor-Boveri-Institut für Biowissenschaften
Universität Würzburg
https://opus.bibliothek.uni-wuerzburg.de/files/5711/Sebald07.pdf
15857
2017
eng
e0181884
7
12
article
1
2018-03-07
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The nuclear proteome of Trypanosoma brucei
Trypanosoma brucei is a protozoan flagellate that is transmitted by tsetse flies into the mammalian bloodstream. The parasite has a huge impact on human health both directly by causing African sleeping sickness and indirectly, by infecting domestic cattle. The biology of trypanosomes involves some highly unusual, nuclear-localised processes. These include polycistronic transcription without classical promoters initiated from regions defined by histone variants, trans-splicing of all transcripts to the exon of a spliced leader RNA, transcription of some very abundant proteins by RNA polymerase I and antigenic variation, a switch in expression of the cell surface protein variants that allows the parasite to resist the immune system of its mammalian host. Here, we provide the nuclear proteome of procyclic Trypanosoma brucei, the stage that resides within the tsetse fly midgut. We have performed quantitative label-free mass spectrometry to score 764 significantly nuclear enriched proteins in comparison to whole cell lysates. A comparison with proteomes of several experimentally characterised nuclear and non-nuclear structures and pathways confirmed the high quality of the dataset: the proteome contains about 80% of all nuclear proteins and less than 2% false positives. Using motif enrichment, we found the amino acid sequence KRxR present in a large number of nuclear proteins. KRxR is a sub-motif of a classical eukaryotic monopartite nuclear localisation signal and could be responsible for nuclear localization of proteins in Kinetoplastida species. As a proof of principle, we have confirmed the nuclear localisation of six proteins with previously unknown localisation by expressing eYFP fusion proteins. While proteome data of several T. brucei organelles have been published, our nuclear proteome closes an important gap in knowledge to study trypanosome biology, in particular nuclear-related processes.
PLoS ONE
10.1371/journal.pone.0181884
urn:nbn:de:bvb:20-opus-158572
PLoS ONE 12(7): e0181884 (2017). DOI: 10.1371/journal.pone.0181884
CC BY: Creative-Commons-Lizenz: Namensnennung 4.0 International
Carina Goos
Mario Dejung
Christian J. Janzen
Falk Butter
Susanne Kramer
eng
uncontrolled
Trypanosoma
eng
uncontrolled
gambiense
eng
uncontrolled
Trypanosoma brucei
eng
uncontrolled
proteomes
eng
uncontrolled
yellow fluorescent protein
eng
uncontrolled
mitochondria
eng
uncontrolled
protein structure
eng
uncontrolled
histones
Mikroorganismen, Pilze, Algen
open_access
Theodor-Boveri-Institut für Biowissenschaften
Förderzeitraum 2017
Universität Würzburg
https://opus.bibliothek.uni-wuerzburg.de/files/15857/Goos_Plos_One.pdf