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Suppahia A, Itagi P, Burris A, et al. Cooperativity in Proteasome Core Particle Maturation. iScience. 2020;23(5):101090doi: 10.1016/j.isci.2020.101090.
Suppahia, A., Itagi, P., Burris, A., Kim, F. M. G., Vontz, A., Kante, A., Kim, S., Im, W., Deeds, E. J., & Roelofs, J. (2020). Cooperativity in Proteasome Core Particle Maturation. iScience, 23(5), 101090. https://doi.org/10.1016/j.isci.2020.101090
Suppahia, Anjana, et al. "Cooperativity in Proteasome Core Particle Maturation." iScience vol. 23,5 (2020): 101090. doi: https://doi.org/10.1016/j.isci.2020.101090
Suppahia A, Itagi P, Burris A, Kim FMG, Vontz A, Kante A, Kim S, Im W, Deeds EJ, Roelofs J. Cooperativity in Proteasome Core Particle Maturation. iScience. 2020 May 22;23(5):101090. doi: 10.1016/j.isci.2020.101090. Epub 2020 Apr 22. PMID: 32380419; PMCID: PMC7210456.
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iScience. 2020 May 22;23(5):101090. doi: 10.1016/j.isci.2020.101090. Epub 2020 Apr 22.

Cooperativity in Proteasome Core Particle Maturation.

iScience

Anjana Suppahia, Pushpa Itagi, Alicia Burris, Faith Mi Ge Kim, Alexander Vontz, Anupama Kante, Seonghoon Kim, Wonpil Im, Eric J Deeds, Jeroen Roelofs

Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA; Molecular, Cellular, and Developmental Biology Program, Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, KS 66506, USA.
  2. Center for Computational Biology, University of Kansas, 2030 Becker Drive, Lawrence, KS 66047, USA; Institute for Quantitative and Computational Biosciences, University of California Los Angeles, Los Angeles, CA 99024, USA.
  3. Molecular, Cellular, and Developmental Biology Program, Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, KS 66506, USA.
  4. Institute for Quantitative and Computational Biosciences, University of California Los Angeles, Los Angeles, CA 99024, USA; Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66047, USA.
  5. Department of Biological Sciences, Lehigh University, Bethlehem, PA 18105, USA.
  6. Department of Biological Sciences, Lehigh University, Bethlehem, PA 18105, USA; Department of Bioengineering, Lehigh University, Bethlehem, PA 18105, USA; Department of Chemistry, Lehigh University, Bethlehem, PA 18105, USA.
  7. Center for Computational Biology, University of Kansas, 2030 Becker Drive, Lawrence, KS 66047, USA; Institute for Quantitative and Computational Biosciences, University of California Los Angeles, Los Angeles, CA 99024, USA; Department of Integrative Biology and Physiology, University of California Los Angeles, Los Angeles, CA 99024, USA. Electronic address: [email protected].
  8. Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA; Molecular, Cellular, and Developmental Biology Program, Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, KS 66506, USA. Electronic address: [email protected].

PMID: 32380419 PMCID: PMC7210456 DOI: 10.1016/j.isci.2020.101090

Abstract

Proteasomes are multi-subunit protease complexes found in all domains of life. The maturation of the core particle (CP), which harbors the active sites, involves dimerization of two half CPs (HPs) and an autocatalytic cleavage that removes β propeptides. How these steps are regulated remains poorly understood. Here, we used the Rhodococcus erythropolis CP to dissect this process in vitro. Our data show that propeptides regulate the dimerization of HPs through flexible loops we identified. Furthermore, N-terminal truncations of the propeptides accelerated HP dimerization and decelerated CP auto-activation. We identified cooperativity in autocatalysis and found that the propeptide can be partially cleaved by adjacent active sites, potentially aiding an otherwise strictly autocatalytic mechanism. We propose that cross-processing during bacterial CP maturation is the underlying mechanism leading to the observed cooperativity of activation. Our work suggests that the bacterial β propeptide plays an unexpected and complex role in regulating dimerization and autocatalytic activation.

Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.

Keywords: Biochemistry; Biological Sciences; Microbiology

Conflict of interest statement

Declaration of Interests The authors declare no competing interests.

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