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Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax

David W. Howell, Shang-Pu Tsai, Kelly Churion, Jan Patterson, Colette Abbey, Joshua T. Atkinson, Dustin Porterpan, Yil-Hwan You, Kenith Meissner, Kayla J. Bayless, Sarah E. Bondos

Advanced Functional Materials, Volume: 25, Issue: 37, Pages: 5988 - 5998

Swansea University Author: Kenith Meissner

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DOI (Published version): 10.1002/adfm.201502852

Abstract

The recombinant protein Ultrabithorax (Ubx), a Drosophila melanogaster Hox transcription factor, self-assembles in vitro into biocompatible materials that are remarkably extensible and strong. Here, it is demonstrated that the strength of Ubx materials is due to intermolecular dityrosine bonds. Ubx...

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Published in: Advanced Functional Materials
Published: 2015
Online Access: http://onlinelibrary.wiley.com/doi/10.1002/adfm.201502852/full
URI: https://cronfa.swan.ac.uk/Record/cronfa27486
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spelling 2021-01-22T12:10:33.5206165 v2 27486 2016-04-27 Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax 30fdfec0d8b19b59b57a818e054d4af3 Kenith Meissner Kenith Meissner true false 2016-04-27 FGSEN The recombinant protein Ultrabithorax (Ubx), a Drosophila melanogaster Hox transcription factor, self-assembles in vitro into biocompatible materials that are remarkably extensible and strong. Here, it is demonstrated that the strength of Ubx materials is due to intermolecular dityrosine bonds. Ubx materials autofluoresce blue, a characteristic of dityrosine, and bind dityrosine-specific antibodies. Monitoring the fluorescence of reduced Ubx fibers upon oxygen exposure reveals biphasic bond formation kinetics. Two dityrosine bonds in Ubx are identified by site-directed mutagenesis followed by measurements of fiber fluorescence intensity. One bond is located between the N-terminus and the homeodomain (Y4/Y296 or Y12/Y293), and another bond is formed by Y167 and Y240. Fiber fluorescence closely correlates with fiber strength, demonstrating that these bonds are intermolecular. This is the first identification of specific residues that participate in dityrosine bonds in protein-based materials. The percentage of Ubx molecules harboring both bonds can be decreased or increased by mutagenesis, providing an additional mechanism to control the mechanical properties of Ubx materials. Duplication of tyrosine-containing motifs in Ubx increases dityrosine content in Ubx fibers, suggesting these motifs could be inserted in other self-assembling proteins to strengthen the corresponding materials. Journal Article Advanced Functional Materials 25 37 5988 5998 7 10 2015 2015-10-07 10.1002/adfm.201502852 http://onlinelibrary.wiley.com/doi/10.1002/adfm.201502852/full Published in a leading materials journal (Impact factor: 11.8), this work elucidates the mechanism for the simple, self assembly of structures from natural protein monomer and enables rational design of structures, fibres and sheets, that are highly elastic, tunable and can be functionalised for numerous applications in biomedicine and sensing. This is a long term interdisciplinary, international collaboration with a molecular biochemist (Bondos, TAMU) and a physiologist (Bayless, TAMU) where the Meissner group provides optical and engineering expertise. This publication follows from earlier high impact publications on the basic characterisation of the structures (Biomacromolecules 2011 and Biomacromolecules 2010). COLLEGE NANME Science and Engineering - Faculty COLLEGE CODE FGSEN Swansea University 2021-01-22T12:10:33.5206165 2016-04-27T16:35:42.8310638 Faculty of Science and Engineering School of Engineering and Applied Sciences - Uncategorised David W. Howell 1 Shang-Pu Tsai 2 Kelly Churion 3 Jan Patterson 4 Colette Abbey 5 Joshua T. Atkinson 6 Dustin Porterpan 7 Yil-Hwan You 8 Kenith Meissner 9 Kayla J. Bayless 10 Sarah E. Bondos 11
title Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax
spellingShingle Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax
Kenith Meissner
title_short Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax
title_full Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax
title_fullStr Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax
title_full_unstemmed Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax
title_sort Identification of Multiple Dityrosine Bonds in Materials Composed of the Drosophila Protein Ultrabithorax
author_id_str_mv 30fdfec0d8b19b59b57a818e054d4af3
author_id_fullname_str_mv 30fdfec0d8b19b59b57a818e054d4af3_***_Kenith Meissner
author Kenith Meissner
author2 David W. Howell
Shang-Pu Tsai
Kelly Churion
Jan Patterson
Colette Abbey
Joshua T. Atkinson
Dustin Porterpan
Yil-Hwan You
Kenith Meissner
Kayla J. Bayless
Sarah E. Bondos
format Journal article
container_title Advanced Functional Materials
container_volume 25
container_issue 37
container_start_page 5988
publishDate 2015
institution Swansea University
doi_str_mv 10.1002/adfm.201502852
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Engineering and Applied Sciences - Uncategorised{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Engineering and Applied Sciences - Uncategorised
url http://onlinelibrary.wiley.com/doi/10.1002/adfm.201502852/full
document_store_str 0
active_str 0
description The recombinant protein Ultrabithorax (Ubx), a Drosophila melanogaster Hox transcription factor, self-assembles in vitro into biocompatible materials that are remarkably extensible and strong. Here, it is demonstrated that the strength of Ubx materials is due to intermolecular dityrosine bonds. Ubx materials autofluoresce blue, a characteristic of dityrosine, and bind dityrosine-specific antibodies. Monitoring the fluorescence of reduced Ubx fibers upon oxygen exposure reveals biphasic bond formation kinetics. Two dityrosine bonds in Ubx are identified by site-directed mutagenesis followed by measurements of fiber fluorescence intensity. One bond is located between the N-terminus and the homeodomain (Y4/Y296 or Y12/Y293), and another bond is formed by Y167 and Y240. Fiber fluorescence closely correlates with fiber strength, demonstrating that these bonds are intermolecular. This is the first identification of specific residues that participate in dityrosine bonds in protein-based materials. The percentage of Ubx molecules harboring both bonds can be decreased or increased by mutagenesis, providing an additional mechanism to control the mechanical properties of Ubx materials. Duplication of tyrosine-containing motifs in Ubx increases dityrosine content in Ubx fibers, suggesting these motifs could be inserted in other self-assembling proteins to strengthen the corresponding materials.
published_date 2015-10-07T03:33:19Z
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score 11.013148

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