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Cited by 13Photosynthetic Processes and MechanismsRNA Research and SplicingRNA and protein synthesis mechanisms

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The RRM domain–containing protein Rbp3 interacts with ribosomes and the 3’ ends of mRNAs encoding photosynthesis proteins

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Hemm, Luisa, Lichtenberg, Elisabeth, Tholen, Stefan, Reimann, Viktoria, Kakazu, Kenta, Machida, Sotaro, Mahbub, Moontaha, Schilling, Oliver, Wilde, Annegret, Watanabe, Satoru, Mullineaux, Conrad W., Hess, Wolfgang R.·2025·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.2506275122PMC PMC12232666

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Abstract

RNA recognition motif (RRM) domain proteins are crucial RNA-binding proteins across all domains of life. In cyanobacteria, single RRM domain proteins are involved in mRNA targeting to the thylakoid membrane and acclimation to certain stress conditions, but many details of their physiological functions and molecular targets have remained unknown. The model cyanobacterium Synechocystis sp. PCC 6803 has a family of three genes encoding the RRM domain–containing proteins Rbp1, Rbp2, and Rbp3. Here, we verified the RNA-binding activity of Rbp3 in vivo and show that cells of a Δ rbp3 deletion strain had a lower photosystem (PS) I:PSII ratio and decreased pigment content and were significantly smaller than wild-type cells. To identify the set of interacting molecules, coimmunoprecipitation experiments were performed with a strain expressing a C-terminally FLAG-tagged Rbp3. Mass spectrometry of the elution fraction suggested physical proximity between Rbp3, ribosomes, and a very small number of other proteins. The most highly enriched transcript in the coeluting RNA fraction was the psaAB mRNA. This was corroborated by fluorescent in situ hybridization analyses showing decreased psaA mRNA signals in Δ rbp3 , and colocalization with Rbp3 fusions to the green fluorescent protein (GFP) in the wild type. Other mRNAs coenriched with Rbp3 encode thylakoid, plasma membrane, and carboxysome proteins. Binding assays using Bio-layer Interferometry validated the Rbp3- psaAB mRNA interaction, indicating a preference for folded RNA segments near or overlapping the respective stop codons.

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Metadata

Authors
Hemm, L., Lichtenberg, E., Tholen, S., Reimann, V., Kakazu, K., Machida, S., Mahbub, M., Schilling, O., Wilde, A., Watanabe, S., Mullineaux, C. W., & Hess, W. R.
Affiliations
  • University of Freiburg (DE)
  • Tokyo University of Agriculture (JP)
  • Queen Mary University of London (GB)
Corresponding author
Hess, Wolfgang R.
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2025-06-24
Volume
122
Issue
26
Pages
e2506275122-e2506275122
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.2506275122
PMC
PMC12232666
OpenAlex
W4411582702
Cited by
13
References
2
Citations by year
2026: 7 · 2025: 5
FWCI
3.56
Type
journal article
Language
en
Open access
Licence
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
Funders
  • Deutsche Forschungsgemeinschaft (322977937/GRK2344, HE 2544/22-1, SCHI 871/11-1)
  • UKRI | Biotechnology and Biological Sciences Research Council (BB/W001012/1)
  • Medical Faculty of the University of Freiburg (2021/A3-Sch)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
RBP3, RNA-binding proteins, Synechocystis sp. PCC 6803, cyanobacteria, ribosome binding, mRNA localization, RNA-protein interactions
MeSH terms
RNA Recognition Motif, Bacterial Proteins, Photosynthesis, Protein Binding, Ribosomes, RNA, Messenger, RNA-Binding Proteins, Synechocystis

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