DnaK and DnaJ proteins from Hsp70/40 family are involved in Rubisco biosynthesis in Synechocystis sp. PCC6803 and sustain the enzyme assembly in a heterologous system
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Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the first step of carbon fixation performed by photosynthetic organisms. Form I of this enzyme found in plants and cyanobacteria is composed of eight large (RbcL) and eight small (RbcS) subunits. To form a functional enzyme, Rubisco subunits need to be properly folded, with the assistance of cellular chaperone machinery, and consecutively assembled in a strictly orchestrated manner, with the help of multiple auxiliary factors. In recent years, multiple Rubisco assembly chaperones and their function in enzyme biogenesis have been extensively characterized. Little is known about the potential specialized factors involved in Rubisco subunits folding at the pre-chaperonin stage, yet this knowledge is greatly needed for the fast and efficient testing of new Rubisco variants. Synechococcus sp. PCC 6803 Rubisco shows limited solubility and a lack of assembly in the Escherichia coli expression system. In this study, we aim to identify which additional chaperones are necessary and sufficient in sustaining the heterologous assembly of native Rubisco. Our findings prove that upon the introduction of Synechocystis DnaK2 to the E. coli system, RbcL is produced in soluble form. The addition of specific DnaJ (Sll1384) enhances this effect. We explain these combined effects based on binding constancies, measured for particular partners in vitro, as well as our analysis of the putative tertiary structure of the proteins. Our results have potential implications for Rubisco engineering.
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DnaK/DnaJ-family chaperones from Synechocystis sp. PCC 6803 have been shown to support soluble Rubisco assembly in a heterologous system.
“for example, DnaK/DnaJ-family chaperones from Synechocystis sp. PCC 6803 have been shown to support soluble Rubisco assembly in a heterologous system [166].”
From Cyanobacteria as a Photosynthetic Chassis for Metabolic Pathway Engineering with Heterologous Gene Expression (2026) · cites this paper as [166]
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“Chaperone co-expression can improve solubility and assembly of difficult proteins, particularly multi-subunit or aggregation-prone enzymes; for example, DnaK/DnaJ-family chaperones from Synechocystis sp. PCC 6803 have been shown to support soluble Rubisco assembly in a heterologous system [166].”
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- Authors
- Rydzy, M., Kolesiński, P., Szczepaniak, A., & Grzyb, J.
- Affiliations
- University of Wrocław (PL)
- Corresponding author
- Grzyb, Joanna
- Venue
- BMC Plant Biology
- Published
- 2023-02-23
- Volume
- 23
- Issue
- 1
- Pages
- 109-109
- ISSN
- 1471-2229 (ISSN-L)
- PMC
- PMC9948308
- OpenAlex
- W4321482809
- Cited by
- 8
- References
- 34
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 2 · 2023: 2
- FWCI
- 0.71
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- BMC Plant Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Narodowe Centrum Nauki (2019/33/N/NZ3/01168)
- Topics
- 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
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- Rubisco assembly, DnaK, Hsp40, Synechocystis sp. PCC 6803, heterologous expression in Escherichia coli, chaperone binding, Rubisco engineering, cyanobacterial photosynthesis
- MeSH terms
- Bacterial Proteins, Ribulose-Bisphosphate Carboxylase, Molecular Chaperones, HSP70 Heat-Shock Proteins, Escherichia coli Proteins, Synechocystis, HSP40 Heat-Shock Proteins
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