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Tunable hetero-assembly of a plant pseudoenzyme-enzyme complex

Irina V. Novikova, Mowei Zhou, Chen Du, Marcelina Parra, Doo Nam Kim, Zachary L. VanAernum, Jared B. Shaw, Hanjo Hellmann, Vicki H. Wysocki, James E. Evans
doi: https://doi.org/10.1101/717082
Irina V. Novikova
1Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA, USA
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  • For correspondence: james.evans@pnnl.gov irina.novikova@pnnl.gov mowei.zhou@pnnl.gov
Mowei Zhou
1Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA, USA
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  • For correspondence: james.evans@pnnl.gov irina.novikova@pnnl.gov mowei.zhou@pnnl.gov
Chen Du
2Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA
3Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA
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Marcelina Parra
4School of Biological Sciences, Washington State University, Pullman, WA, 99164, USA
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Doo Nam Kim
5Biological Science Division, Pacific Northwest National Laboratory, Richland, WA, USA
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Zachary L. VanAernum
2Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA
3Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA
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Jared B. Shaw
1Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA, USA
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Hanjo Hellmann
4School of Biological Sciences, Washington State University, Pullman, WA, 99164, USA
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Vicki H. Wysocki
2Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA
3Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA
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James E. Evans
1Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA, USA
4School of Biological Sciences, Washington State University, Pullman, WA, 99164, USA
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  • For correspondence: james.evans@pnnl.gov irina.novikova@pnnl.gov mowei.zhou@pnnl.gov
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Abstract

Pseudoenzymes have emerged as key regulatory elements in all kingdoms of life despite being catalytically non-active. Yet many factors defining why one protein is active while its homolog is inactive remain uncertain. For pseudoenzyme-enzyme pairs, the similarity of both subunits can often hinder conventional characterization approaches. In plants, a pseudoenzyme PDX1.2 positively regulates vitamin B6 production by association with its active catalytic homologs such as PDX1.3 through an unknown mechanism. Here we used an integrative experimental approach to learn that such pseudoenzyme-enzyme pair associations result in hetero-complexes of variable stoichiometry, which are unexpectedly tunable. We also present the atomic structure of the PDX1.2 pseudoenzyme as well as the population averaged PDX1.2-PDX1.3 pseudoenzyme-enzyme pair. Finally, we dissected hetero-dodecamers of each stoichiometry to understand the arrangement of monomers in the hetero-complexes and identified symmetry- imposed preferences in PDX1.2-PDX1.3 interactions. Our results provide a new model of pseudoenzyme-enzyme interactions and their native heterogeneity.

Competing Interest Statement

The authors have declared no competing interest.

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  • New data has been incorporated

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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. It is made available under a CC-BY-ND 4.0 International license.
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Posted May 09, 2020.
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Tunable hetero-assembly of a plant pseudoenzyme-enzyme complex
Irina V. Novikova, Mowei Zhou, Chen Du, Marcelina Parra, Doo Nam Kim, Zachary L. VanAernum, Jared B. Shaw, Hanjo Hellmann, Vicki H. Wysocki, James E. Evans
bioRxiv 717082; doi: https://doi.org/10.1101/717082
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Tunable hetero-assembly of a plant pseudoenzyme-enzyme complex
Irina V. Novikova, Mowei Zhou, Chen Du, Marcelina Parra, Doo Nam Kim, Zachary L. VanAernum, Jared B. Shaw, Hanjo Hellmann, Vicki H. Wysocki, James E. Evans
bioRxiv 717082; doi: https://doi.org/10.1101/717082

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