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Biotinylation by antibody recognition - A novel method for proximity labeling

View ORCID ProfileDaniel Z Bar, Kathleen Atkatsh, Urraca Tavarez, Michael R Erdos, Yosef Gruenbaum, Francis S Collins
doi: https://doi.org/10.1101/069187
Daniel Z Bar
1National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
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Kathleen Atkatsh
1National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
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Urraca Tavarez
1National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
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Michael R Erdos
1National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
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Yosef Gruenbaum
2Department of Genetics, Institute of Life Sciences, The Hebrew University of Jerusalem, Givat Ram, Jerusalem 9190401, Israel
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Francis S Collins
1National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
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Abstract

Identification of protein-protein interactions is a major goal of biological research. Despite technical advances over the last two decades, important but still largely unsolved challenges include the high-throughput detection of interactions directly from primary tissue and the identification of interactors of insoluble proteins that form higher-order structures. We have developed a novel, proximity-based labeling approach that uses antibodies to guide biotin deposition onto adjacent proteins in fixed cells and primary tissues. We used this method to profile the dynamic interactome of lamin A/C in multiple cell and tissue types under various treatment conditions. Our results suggest a considerable variation in the composition of the nuclear envelope of different tissues. Of note, DNA damage response proteins Ku70 and Ku80 are more abundant in the vicinity of lamin A/C after thermal stress. This increased affinity also applies to the progerin isoform, potentially contributing to the premature aging phenotype of Hutchinson-Gilford progeria syndrome. The ability to detect protein-protein interactions in intact tissues, and to compare affinities quantitatively under different conditions or in the presence of disease mutations, can provide a new window into cell biology and disease pathogenesis.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted August 11, 2016.
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Biotinylation by antibody recognition - A novel method for proximity labeling
Daniel Z Bar, Kathleen Atkatsh, Urraca Tavarez, Michael R Erdos, Yosef Gruenbaum, Francis S Collins
bioRxiv 069187; doi: https://doi.org/10.1101/069187
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Biotinylation by antibody recognition - A novel method for proximity labeling
Daniel Z Bar, Kathleen Atkatsh, Urraca Tavarez, Michael R Erdos, Yosef Gruenbaum, Francis S Collins
bioRxiv 069187; doi: https://doi.org/10.1101/069187

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