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Berlin Brandenburg

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  • 1
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 31 May 2011, Vol.108(22), pp.8919-20
    Description: Author contributions: C.F. and H.L wrote the paper.
    Keywords: DNA Methylation ; DNA (Cytosine-5-)-Methyltransferases -- Chemistry
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 2
    Language: English
    In: Science, March 25, 2011, Vol.331(6024), p.1616(5)
    Description: After partitioning of cytoplasrnic contents by cleavage furrow ingression, animal cells remain connected by an intercellular bridge, which subsequently splits by abscission. Here, we examined intermediate stages of abscission in human cells by using five imaging, three- dimensional structured illumination microscopy, and electron tomography. We identified helices of 17-nanometer-diameter filaments, which narrowed the cortex of the intercellular bridge to a single stalk. The endosomal sorting complex required for transport (ESCRT)-III co-locatized with constriction zones and was required for assembly of 17-nanometer-diameter filaments. Simuttaneous spastin-mediated removal of underlying microtubules enabled full constriction at the abscission site. The identification of contractile filament helices at the intercellular bridge has broad implications for the understanding of cell division and of ESCRT-III- mediated fission of large membrane structures. 10.1126/science.1201847
    Keywords: Cell Division -- Genetic Aspects ; Protein Structure -- Research
    ISSN: 0036-8075
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  • 3
    Language: English
    In: Biochemical and Biophysical Research Communications, 23 March 2012, Vol.419(4), pp.698-702
    Description: ► Characterization of the proliferating cell nuclear antigen in (TbPCNA). ► TbPCNA is a suitable marker to detect replication in . ► TbPCNA distribution and regulation is different compared to closely related parasites and . As in most eukaryotic cells, replication is regulated by a conserved group of proteins in the early-diverged parasite . Only a few components of the replication machinery have been described in this parasite and regulation, sub-nuclear localization and timing of replication are not well understood. We characterized the proliferating cell nuclear antigen in (TbPCNA) to establish a spatial and temporal marker for replication. Interestingly, PCNA distribution and regulation is different compared to the closely related parasites and . TbPCNA foci are clearly detectable during S phase of the cell cycle but in contrast to they are not preferentially located at the nuclear periphery. Furthermore, PCNA seems to be degraded when cells enter G2 phase in suggesting different modes of replication regulation or functions of PCNA in these closely related eukaryotes.
    Keywords: Pcna ; Replication ; S Phase Marker ; Cell Cycle Regulation ; Trypanosoma Brucei ; Biology ; Chemistry ; Anatomy & Physiology
    ISSN: 0006-291X
    E-ISSN: 1090-2104
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  • 4
    Language: English
    In: The Journal of cell biology, 26 July 2010, Vol.190(2), pp.165-75
    Description: For centuries, cell biology has been based on light microscopy and at the same time been limited by its optical resolution. However, several new technologies have been developed recently that bypass this limit. These new super-resolution technologies are either based on tailored illumination, nonlinear fluorophore responses, or the precise localization of single molecules. Overall, these new approaches have created unprecedented new possibilities to investigate the structure and function of cells.
    Keywords: Microscopy, Fluorescence -- Methods
    ISSN: 00219525
    E-ISSN: 1540-8140
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  • 5
    Language: English
    In: The Journal of cell biology, 08 June 2015, Vol.209(5), pp.633-44
    Description: Antibodies are key reagents to investigate cellular processes. The development of recombinant antibodies and binders derived from natural protein scaffolds has expanded traditional applications, such as immunofluorescence, binding arrays, and immunoprecipitation. In addition, their small size and high stability in ectopic environments have enabled their use in all areas of cell research, including structural biology, advanced microscopy, and intracellular expression. Understanding these novel reagents as genetic modules that can be integrated into cellular pathways opens up a broad experimental spectrum to monitor and manipulate cellular processes.
    Keywords: Single-Domain Antibodies
    ISSN: 00219525
    E-ISSN: 1540-8140
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  • 6
    Language: English
    In: PLoS ONE, 01 January 2014, Vol.9(12), p.e115049
    Description: Quantitative proteome research is greatly promoted by high-resolution parallel format assays. A characterization of protein complexes based on binding forces offers an unparalleled dynamic range and allows for the effective discrimination of non-specific interactions. Here we present a DNA-based Molecular Force Assay to quantify protein-protein interactions, namely the bond between different variants of GFP and GFP-binding nanobodies. We present different strategies to adjust the maximum sensitivity window of the assay by influencing the binding strength of the DNA reference duplexes. The binding of the nanobody Enhancer to the different GFP constructs is compared at high sensitivity of the assay. Whereas the binding strength to wild type and enhanced GFP are equal within experimental error, stronger binding to superfolder GFP is observed. This difference in binding strength is attributed to alterations in the amino acids that form contacts according to the crystal structure of the initial wild type GFP-Enhancer complex. Moreover, we outline the potential for large-scale parallelization of the assay.
    Keywords: Sciences (General)
    E-ISSN: 1932-6203
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  • 7
    Language: English
    In: Science (New York, N.Y.), 25 March 2011, Vol.331(6024), pp.1616-20
    Description: After partitioning of cytoplasmic contents by cleavage furrow ingression, animal cells remain connected by an intercellular bridge, which subsequently splits by abscission. Here, we examined intermediate stages of abscission in human cells by using live imaging, three-dimensional structured illumination microscopy, and electron tomography. We identified helices of 17-nanometer-diameter filaments, which narrowed the cortex of the intercellular bridge to a single stalk. The endosomal sorting complex required for transport (ESCRT)-III co-localized with constriction zones and was required for assembly of 17-nanometer-diameter filaments. Simultaneous spastin-mediated removal of underlying microtubules enabled full constriction at the abscission site. The identification of contractile filament helices at the intercellular bridge has broad implications for the understanding of cell division and of ESCRT-III-mediated fission of large membrane structures.
    Keywords: Cell Division ; Endosomal Sorting Complexes Required for Transport -- Chemistry ; Microtubules -- Metabolism
    ISSN: 00368075
    E-ISSN: 1095-9203
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  • 8
    In: Nature, 2017
    Description: Cytosolic DNA arising from intracellular pathogens triggers a powerful innate immune response. It is sensed by cyclic GMP-AMP synthase (cGAS), which elicits the production of type I interferons by generating the second messenger 2'3'-cyclic-GMP-AMP (cGAMP). Endogenous nuclear or mitochondrial DNA can also be sensed by cGAS under certain conditions, resulting in sterile inflammation. The cGAS dimer binds two DNA ligands shorter than 20 base pairs side-by-side, but 20-base-pair DNA fails to activate cGAS in vivo and is a poor activator in vitro. Here we show that cGAS is activated in a strongly DNA length-dependent manner both in vitro and in human cells. We also show that cGAS dimers form ladder-like networks with DNA, leading to cooperative sensing of DNA length: assembly of the pioneering cGAS dimer between two DNA molecules is ineffective; but, once formed, it prearranges the flanking DNA to promote binding of subsequent cGAS dimers. Remarkably, bacterial and mitochondrial nucleoid proteins HU and mitochondrial transcription factor A (TFAM), as well as high-mobility group box 1 protein (HMGB1), can strongly stimulate long DNA sensing by cGAS. U-turns and bends in DNA induced by these proteins pre-structure DNA to nucleate cGAS dimers. Our results suggest a nucleation-cooperativity-based mechanism for sensitive detection of mitochondrial DNA and pathogen genomes, and identify HMGB/TFAM proteins as DNA-structuring host factors. They provide an explanation for the peculiar cGAS dimer structure and suggest that cGAS preferentially binds incomplete nucleoid-like structures or bent DNA.
    Keywords: DNA -- Chemistry ; DNA-Binding Proteins -- Metabolism ; Hmgb Proteins -- Metabolism ; High Mobility Group Proteins -- Metabolism ; Mitochondrial Proteins -- Metabolism ; Nucleotidyltransferases -- Metabolism ; Transcription Factors -- Metabolism;
    ISSN: 0028-0836
    E-ISSN: 1476-4687
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  • 9
    Language: English
    In: 2012, Vol.7(11), p.e50026
    Description: In basic and applied HIV research, reliable detection of viral components is crucial to monitor progression of infection. While it is routine to detect structural viral proteins in vitro for diagnostic purposes, it previously remained impossible to directly and dynamically visualize HIV in living cells without genetic modification of the virus. Here, we describe a novel fluorescent biosensor to dynamically trace HIV-1 morphogenesis in living cells. We generated a camelid single domain antibody that specifically binds the HIV-1 capsid protein (CA) at subnanomolar affinity and fused it to fluorescent proteins. The resulting fluorescent chromobody specifically recognizes the CA-harbouring HIV-1 Gag precursor protein in living cells and is applicable in various advanced light microscopy systems. Confocal live cell microscopy and super-resolution microscopy allowed detection and dynamic tracing of individual virion assemblies at the plasma membrane. The analysis of subcellular binding kinetics showed cytoplasmic antigen recognition and incorporation into virion assembly sites. Finally, we demonstrate the use of this new reporter in automated image analysis, providing a robust tool for cell-based HIV research.
    Keywords: Research Article ; Biology ; Medicine ; Immunology ; Virology ; Infectious Diseases ; Biotechnology ; Cell Biology ; Biochemistry
    E-ISSN: 1932-6203
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  • 10
    Language: English
    In: The Journal of biological chemistry, 20 February 2015, Vol.290(8), pp.4801-12
    Description: TET proteins oxidize 5-methylcytosine to 5-hydroxymethylcytosine, 5-formylcytosine, and 5-carboxylcytosine and thus provide a possible means for active DNA demethylation in mammals. Although their catalytic mechanism is well characterized and the catalytic dioxygenase domain is highly conserved, the function of the regulatory regions (the N terminus and the low-complexity insert between the two parts of the dioxygenase domains) is only poorly understood. Here, we demonstrate that TET proteins are subject to a variety of post-translational modifications that mostly occur at these regulatory regions. We mapped TET modification sites at amino acid resolution and show for the first time that TET1, TET2, and TET3 are highly phosphorylated. The O-linked GlcNAc transferase, which we identified as a strong interactor with all three TET proteins, catalyzes the addition of a GlcNAc group to serine and threonine residues of TET proteins and thereby decreases both the number of phosphorylation sites and site occupancy. Interestingly, the different TET proteins display unique post-translational modification patterns, and some modifications occur in distinct combinations. In summary, our results provide a novel potential mechanism for TET protein regulation based on a dynamic interplay of phosphorylation and O-GlcNAcylation at the N terminus and the low-complexity insert region. Our data suggest strong cross-talk between the modification sites that could allow rapid adaption of TET protein localization, activity, or targeting due to changing environmental conditions as well as in response to external stimuli.
    Keywords: 5-Hydroxymethylcytosine (5-Hmc) ; Dioxygenase ; Epigenetics ; O-Linked N-Acetylglucosamine (O-Glcnac) ; Ogt ; Phosphorylation ; Post-Translational Modification (Ptm) ; Tet Proteins ; DNA-Binding Proteins -- Metabolism ; Dioxygenases -- Metabolism ; N-Acetylglucosaminyltransferases -- Metabolism ; Protein Processing, Post-Translational -- Physiology ; Proto-Oncogene Proteins -- Metabolism
    E-ISSN: 1083-351X
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