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Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats

Sara Sajko, Irina Grishkovskaya, Julius Kostan, Melissa Graewert, Kim Setiawan, Linda Trübestein, Korbinian Niedermüller, View ORCID ProfileCharlotte Gehin, Antonio Sponga, Martin Puchinger, Anne-Claude Gavin, Dimitri Svergun, Tom Leonard, Terry K. Smith, View ORCID ProfileBrooke Morriswood, Kristina Djinovic-Carugo
doi: https://doi.org/10.1101/826180
Sara Sajko
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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Irina Grishkovskaya
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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Julius Kostan
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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Melissa Graewert
2European Molecular Biology Laboratory, Hamburg Unit, c/o DESY, Notkestrasse 85, 22607 Hamburg, Germany
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Kim Setiawan
3Department of Cell and Developmental Biology, Biocenter, University of Würzburg, 97074 Würzburg, Germany
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Linda Trübestein
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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Korbinian Niedermüller
3Department of Cell and Developmental Biology, Biocenter, University of Würzburg, 97074 Würzburg, Germany
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Charlotte Gehin
4European Molecular Biology Laboratory, Meyerhofstraße 1, 69117 Heidelberg, Germany
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  • ORCID record for Charlotte Gehin
Antonio Sponga
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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Martin Puchinger
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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Anne-Claude Gavin
4European Molecular Biology Laboratory, Meyerhofstraße 1, 69117 Heidelberg, Germany
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Dimitri Svergun
2European Molecular Biology Laboratory, Hamburg Unit, c/o DESY, Notkestrasse 85, 22607 Hamburg, Germany
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Tom Leonard
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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Terry K. Smith
5School of Biology, BSRC, University of St. Andrews, North Haugh, St. Andrews, Fife KY16 9ST, UK
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Brooke Morriswood
3Department of Cell and Developmental Biology, Biocenter, University of Würzburg, 97074 Würzburg, Germany
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  • For correspondence: brooke.morriswood@uni-wuerzburg.de kristina.djinovic@univie.ac.at
Kristina Djinovic-Carugo
1Department of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
6Department of Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia
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  • For correspondence: brooke.morriswood@uni-wuerzburg.de kristina.djinovic@univie.ac.at
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ABSTRACT

MORN (membrane occupation and recognition nexus) repeat proteins have a wide taxonomic distribution, being found in both prokaryotes and eukaryotes. Despite this ubiquity, they remain poorly characterised at both a structural and a functional level compared to other common repeat motifs such as leucine-rich repeats, armadillo repeats, WD40 repeats, and ankyrin repeats. In functional terms, they are often assumed to be lipid-binding modules that mediate membrane targeting, but direct evidence for this role is actually lacking. This putative activity was addressed by focusing on a protein composed solely of MORN repeats - Trypanosoma brucei MORN1. No evidence for binding to membranes or lipid vesicles by TbMORN1 either in vivo or in vitro could be obtained. TbMORN1 did interact with individual phospholipids, but it remains unclear if this was physiological or an artefact. High- and low-resolution structures of the MORN1 protein from Trypanosoma brucei and homologous proteins from the parasites Toxoplasma gondii and Plasmodium falciparum were obtained using a combination of macromolecular crystallography, small-angle X-ray scattering, and electron microscopy. The structures indicated that MORN repeats can mediate homotypic interactions, and can function as both dimerisation and oligomerisation devices.

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Posted October 31, 2019.
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Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats
Sara Sajko, Irina Grishkovskaya, Julius Kostan, Melissa Graewert, Kim Setiawan, Linda Trübestein, Korbinian Niedermüller, Charlotte Gehin, Antonio Sponga, Martin Puchinger, Anne-Claude Gavin, Dimitri Svergun, Tom Leonard, Terry K. Smith, Brooke Morriswood, Kristina Djinovic-Carugo
bioRxiv 826180; doi: https://doi.org/10.1101/826180
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Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats
Sara Sajko, Irina Grishkovskaya, Julius Kostan, Melissa Graewert, Kim Setiawan, Linda Trübestein, Korbinian Niedermüller, Charlotte Gehin, Antonio Sponga, Martin Puchinger, Anne-Claude Gavin, Dimitri Svergun, Tom Leonard, Terry K. Smith, Brooke Morriswood, Kristina Djinovic-Carugo
bioRxiv 826180; doi: https://doi.org/10.1101/826180

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