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Cited by 1Photosynthetic Processes and MechanismsRNA Research and SplicingPlant Molecular Biology Research

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Maturase K forms a plastidial splicing complex with a neofunctionalized branching enzyme

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Liang, Yuanyuan, Gao, Yang, Fontana, Andrea, Abt, Melanie, Gicgier, Adam, Gehring, Muriel, Liu, Chun, Sharma, Mayank, Zoschke, Reimo, Zeeman, Samuel C., Pfister, Barbara·2026·Nature Communications
DOI 10.1038/s41467-026-70734-3

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Abstract

Chloroplast group IIA introns originate from bacterial ribozymes. Their splicing requires the splicing factor Maturase K (MatK). MatK, however, has been difficult to functionally analyze, as it appears essential for plant viability and is encoded in the chloroplast genome. Here we identified a heteromultimeric complex comprising MatK and three other essential, plastid-targeted proteins using co-immunoprecipitation experiments in Arabidopsis and tobacco. Among the MatK interactors is a conserved homologue of starch-branching enzymes (BEs), which we named MATURASE K INTERACTING PROTEIN1 (MKIP1). We demonstrate that MKIP1 proteins have lost BE activity and acquired a 150-amino acid insertion that enables direct interaction with MatK’s N-terminus. Immunoprecipitation of Arabidopsis MKIP1 co-precipitates all known MatK intron targets. Inducing MKIP1 silencing in Arabidopsis causes newly emerging leaves to be pale, in which the splicing of MatK intron targets is strongly reduced. Our data suggest that MKIP1 functionally diverged from canonical BEs to facilitate splicing in conjunction with MatK. In turn, the former reverse-transcriptase domain in the N-terminal region of MatK likely has acquired the capacity to interact with other proteins. Potentially, complex formation allowed MatK to diversify its RNA interactions, helping its transition towards a general splicing factor.

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Metadata

Authors
Liang, Y., Gao, Y., Fontana, A., Abt, M., Gicgier, A., Gehring, M., Liu, C., Sharma, M., Zoschke, R., Zeeman, S. C., & Pfister, B.
Affiliations
  • ETH Zurich (CH)
  • Max Planck Institute of Molecular Plant Physiology (DE)
  • John Innes Centre (GB)
  • University of Cambridge (GB)
Corresponding author
Pfister, Barbara
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2026-03-23
Volume
17
Issue
1
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-026-70734-3
OpenAlex
W4406160240
Cited by
1
References
3
FWCI
0.00
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • Apollo (University of Cambridge) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
  • Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by)
  • ETH Zürich Research Collection (cc-by)
Funders
  • EC | Horizon 2020 Framework Programme (847585)
  • Deutsche Forschungsgemeinschaft (ZO 302/5-1)
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 › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Keywords
matK, starch branching enzyme, intron splicing, protein-protein interaction, neofunctionalization, functional divergence, splicing factors, Arabidopsis thaliana
MeSH terms
Chloroplasts, Introns, RNA Splicing, Nicotiana, Arabidopsis, Plastids, Arabidopsis Proteins

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