Cited by 16Protein Structure and DynamicsPhotosynthetic Processes and MechanismsHeat shock proteins research

Orchestration of algal metabolism by protein disorder

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Launay, Hélène, Receveur-Bréchot, Véronique, Carrière, Frédéric, Gontero, Brigitte·2019·Archives of Biochemistry and Biophysics

Abstract

Intrinsically disordered proteins (IDPs) are proteins that provide many functional advantages in a large number of metabolic and signalling pathways. Because of their high flexibility that endows them with pressure-, heat- and acid-resistance, IDPs are valuable metabolic regulators that help algae to cope with extreme conditions of pH, temperature, pressure and light. They have, however, been overlooked in these organisms. In this review, we present some well-known algal IDPs, including the conditionally disordered CP12, a protein involved in the regulation of CO 2 assimilation, as probably the best known example, whose disorder content is strongly dependent on the redox conditions, and the essential pyrenoid component 1 that serves as a scaffold for ribulose-1, 5-bisphosphate carboxylase/oxygenase. We also describe how some enzymes are regulated by protein regions, called intrinsically disordered regions (IDRs), such as ribulose-1, 5-bisphosphate carboxylase/oxygenase activase, the A 2 B 2 form of glyceraldehyde-3-phosphate dehydrogenase and the adenylate kinase. Several molecular chaperones, which are crucial for cell proteostasis, also display significant disorder propensities such as the algal heat shock proteins HSP33, HSP70 and HSP90. This review confirms the wide distribution of IDPs in algae but highlights that further studies are needed to uncover their full role in orchestrating algal metabolism.

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Crossref · 10.1016/j.abb.2019.108070

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  • Unlike many structured protein domains, the function of IDPs/IDRs can persist in extreme environmental conditions.

    “Unlike many structured protein domains, the function of IDPs/IDRs can persist in extreme environmental conditions.”

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Authors
Launay, H., Receveur-Bréchot, V., Carrière, F., & Gontero, B.
Affiliations
Centre National de la Recherche Scientifique (FR)
Corresponding author
Gontero, Brigitte
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
2019-09
Volume
672
Pages
108070
ISSN
0003-9861 (ISSN-L)
OpenAlex
W2968553586
Cited by
16
References
144
Citations by year
2025: 1 · 2024: 1 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 4
FWCI
0.26
Type
journal article
Language
en
Open access
Locations
  • Archives of Biochemistry and Biophysics (acceptedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, other-oa)
  • HAL AMU (submittedVersion)
Funders
  • Centre National de la Recherche Scientifique
  • Aix-Marseille Université (ANR-15-CE05-0021-03)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords
intrinsically disordered proteins, intrinsically disordered regions, algae, algal metabolism, CP12, redox regulation, pyrenoid, Rubisco activase, glyceraldehyde-3-phosphate dehydrogenase, adenylate kinase, molecular chaperones, heat shock proteins, proteostasis, carbon assimilation, protein disorder
MeSH terms
Chlorophyta, Photosynthesis, Molecular Chaperones, Algal Proteins, Microalgae, Intrinsically Disordered Proteins

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