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.
Similar content being viewed by others
Data availability
All data needed to evaluate the conclusions in this paper are present in the paper and/or its supplementary materials. Source Data are provided with this paper. The proteomics data are freely available at the ProteomeXchange Consortium via the PRIDE109 partner repository with the identifiers PXD060108 (https://www.ebi.ac.uk/pride/archive/projects/PXD060108) (IP data of AtMKIP1-YFP), PXD060055 (https://www.ebi.ac.uk/pride/archive/projects/PXD060055) (IP data of NtMatK-HA), PXD069946 (https://www.ebi.ac.uk/pride/archive/projects/PXD069946) (MS/MS analysis of SEC fractions), and PXD067382 (https://www.ebi.ac.uk/pride/archive/projects/PXD067382) (Proteomics after silencing of AtMKIP1 or AtuL4c). The RNA sequencing data of RNAs bound to AtMKIP1-YFP are publicly available at NCBI GEO110 with the accession number GSE284378. Microscopy images are freely available at the ETH Research Collection (https://doi.org/10.3929/ethz-c-000795755). New genetic material (transgenic Arabidopsis and yeast lines) and vectors will be made available to the scientific community upon request. Source data are provided with this paper.
References
Germain, A., Hotto, A. M., Barkan, A. & Stern, D. B. RNA processing and decay in plastids. Wiley Interdiscip. Rev. RNA 4, 295–316 (2013).
Small, I., Melonek, J., Bohne, A. V., Nickelsen, J. & Schmitz-Linneweber, C. Plant organellar RNA maturation. Plant Cell 35, 1727–1751 (2023).
Galej, W. P., Toor, N., Newman, A. J. & Nagai, K. Molecular mechanism and evolution of nuclear pre-mRNA and group II intron splicing: insights from cryo-electron microscopy structures. Chem. Rev. 118, 4156–4176 (2018).
Michel, F., Kazuhiko, U. & Haruo, O. Comparative and functional anatomy of group II catalytic introns - a review. Gene 82, 5–30 (1989).
Toor, N., Keating, K. S., Taylor, S. D. & Pyle, A. M. Crystal structure of a self-spliced group II intron. Science 320, 77–82 (2008).
Matsuura, M., Noah, J. W. & Lambowitz, A. M. Mechanism of maturase-promoted group II intron splicing. EMBO J. 20, 7259–7270 (2001).
Zhao, C. & Pyle, A. M. The group II intron maturase: a reverse transcriptase and splicing factor go hand in hand. Curr. Opin. Struct. Biol. 47, 30–39 (2017).
Cui, X., Matsuura, M., Wang, Q., Ma, H. & Lambowitz, A. M. A group II intron-encoded maturase functions preferentially in cis and requires both the reverse transcriptase and X domains to promote RNA splicing. J. Mol. Biol. 340, 211–231 (2004).
Qu, G. et al. Structure of a group II intron in complex with its reverse transcriptase. Nat. Struct. Mol. Biol. 23, 549–557 (2016).
Xu, L., Liu, T., Chung, K. & Pyle, A. M. Structural insights into intron catalysis and dynamics during splicing. Nature 624, 682–688 (2023).
Haack, D. B., Rudolfs, B., Zhang, C., Lyumkis, D. & Toor, N. Structural basis of branching during RNA splicing. Nat. Struct. Mol. Biol. 31, 179–189 (2024).
Zoschke, R. et al. An organellar maturase associates with multiple group II introns. Proc. Natl. Acad. Sci. USA 107, 3245–3250 (2010).
Muino, J. M. et al. MatK impacts differential chloroplast translation by limiting spliced tRNA-K(UUU) abundance. Plant J. 119, 2737–2752 (2024).
Lemieux, C., Otis, C. & Turmel, M. Comparative chloroplast genome analyses of streptophyte green algae uncover major structural alterations in the Klebsormidiophyceae, Coleochaetophyceae and Zygnematophyceae. Front. Plant Sci. 7, 697 (2016).
Vogel, J. & Börner, T. Lariat formation and a hydrolytic pathway in plant chloroplast group II intron splicing. EMBO J. 21, 3794–3803 (2002).
Schmitz-Linneweber, C., Lampe, M. K., Sultan, L. D. & Ostersetzer-Biran, O. Organellar maturases: a window into the evolution of the spliceosome. Biochim. Biophys. Acta 1847, 798–808 (2015).
Mohr, G., Perlman, P. S. & Lambowitz, A. M. Evolutionary relationships among group II intron-encoded proteins and identification of a conserved domain that may be related to maturase function. Nucleic Acids Res 21, 4991–4997 (1993).
Barthet, M. M. & Hilu, K. W. evaluating evolutionary constraint on the rapidly evolving gene matK using protein composition. J. Mol. Evol. 66, 85–97 (2008).
Hausner, G. et al. Origin and evolution of the chloroplast trnK(matK) intron: A model for evolution of group II intron RNA structures. Mol. Biol. Evol. 23, 380–391 (2006).
Till, B., Schmitz-Linneweber, C., Williams-Carrier, R. & Barkan, A. CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin. RNA 7, 1227–1238 (2001).
Watkins, K. P. et al. A ribonuclease III domain protein functions in group II intron splicing in maize chloroplasts. Plant Cell 19, 2606–2623 (2007).
Kroeger, T. S., Watkins, K. P., Friso, G., Van Wijk, K. J. & Barkan, A. A plant-specific RNA-binding domain revealed through analysis of chloroplast group II intron splicing. Proc. Natl. Acad. Sci. USA 106, 4537–4542 (2009).
Dumez, S. et al. Mutants of Arabidopsis lacking starch branching enzyme II substitute plastidial starch synthesis by cytoplasmic maltose accumulation. Plant Cell 18, 2694–2709 (2006).
Pfister, B. & Zeeman, S. C. Formation of starch in plant cells. Cell. Mol. Life Sci. 73, 2781–2807 (2016).
Pfister, B. et al. Recreating the synthesis of starch granules in yeast. Elife 5, 1–29 (2016).
Wang, X., Xue, L., Sun, J. & Zuo, J. The Arabidopsis BE1 gene, encoding a putative glycoside hydrolase localized in plastids, plays crucial roles during embryogenesis and carbohydrate metabolism. J. Integr. Plant Biol. 52, 273–288 (2010).
Bryant, N., Lloyd, J., Sweeney, C., Myouga, F. & Meinke, D. Identification of nuclear genes encoding chloroplast-localized proteins required for embryo development in Arabidopsis. Plant Physiol. 155, 1678–1689 (2011).
Despres, B., Delseny, M. & Devic, M. Partial complementation of embryo defective mutations: a general strategy to elucidate gene function. Plant J. 27, 149–159 (2001).
Aryamanesh, N. et al. The pentatricopeptide repeat protein EMB2654 is essential for trans-splicing of a chloroplast small ribosomal subunit transcript. Plant Physiol. 173, 1164–1176 (2017).
Yu, H. D. et al. Downregulation of chloroplast RPS1 negatively modulates nuclear heat-responsive expression of HsfA2 and its target genes in Arabidopsis. PLoS Genet 8, e1002669 (2012).
Han, Y., Sun, F. J., Rosales-Mendoza, S. & Korban, S. S. Three orthologs in rice, Arabidopsis, and Populus encoding starch branching enzymes (SBEs) are different from other SBE gene families in plants. Gene 401, 123–130 (2007).
Ball, S., Colleoni, C., Cenci, U., Raj, J. N. & Tirtiaux, C. The evolution of glycogen and starch metabolism in eukaryotes gives molecular clues to understand the establishment of plastid endosymbiosis. J. Exp. Bot. 62, 1775–1801 (2011).
Tetlow, I. J. & Emes, M. J. A review of starch-branching enzymes and their role in amylopectin biosynthesis. IUBMB Life 66, 546–558 (2014).
Pfister, B. et al. Tuning heterologous glucan biosynthesis in yeast to understand and exploit plant starch diversity. BMC Biol. 20, 1–20 (2022).
Kuriki, T., Guan, H., Sivak, M. & Preiss, J. Analysis of the active center of branching enzyme II from maize endosperm. J. Protein Chem. 15, 305–313 (1996).
Funane, K., Libessart, N., Stewart, D., Michishita, T. & Preiss, J. Analysis of essential histidine residues of maize branching enzymes by chemical modification and site-directed mutagenesis. J. Protein Chem. 17, 579–590 (1998).
McBride, A., Ghilagaber, S., Nikolaev, A. & Hardie, D. G. The glycogen-binding domain on the AMPK β subunit allows the kinase to act as a glycogen sensor. Cell Metab. 9, 23–34 (2009).
Seung, D., Schreier, T. B., Bürgy, L., Eicke, S. & Zeeman, S. C. Two plastidial coiled-coil proteins are essential for normal starch granule initiation in Arabidopsis. Plant Cell 30, 1523–1542 (2018).
Berg, M., Rogers, R., Muralla, R. & Meinke, D. Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo development in Arabidopsis. Plant J. 44, 866–878 (2005).
Hayashi-Tsugane, M. et al. A mutable albino allele in rice reveals that formation of thylakoid membranes requires the SNOW-WHITE LEAF1 gene. Plant Cell Physiol. 55, 3–15 (2014).
Wang, Y. et al. Crucial role of SWL1 in chloroplast biogenesis and development in Arabidopsis thaliana. Plant Cell Rep. 43, 1–15 (2024).
Asakura, Y., Bayraktar, O. A. & Barkan, A. Two CRM protein subfamilies cooperate in the splicing of group IIB introns in chloroplasts. RNA 14, 2319–2332 (2008).
Shinozaki, K. et al. The complete nucleotide sequence of the tobacco chloroplast genome: Its gene organization and expression. EMBO J. 5, 2043–2049 (1986).
Vogel, J., Börner, T. & Hess, W. R. Comparative analysis of splicing of the complete set of chloroplast group II introns in three higher plant mutants. Nucleic Acids Res 27, 3866–3874 (1999).
Vogel, J., Hübschmann, T., Börner, T. & Hess, W. R. Splicing and intron-internal RNA editing of trnK-matK transcripts in barley plastids: support for MatK as an essential splice factor. J. Mol. Biol. 270, 179–187 (1997).
Bieri, P., Leibundgut, M., Saurer, M., Boehringer, D. & Ban, N. The complete structure of the chloroplast 70S ribosome in complex with translation factor pY. EMBO J. 36, 475–486 (2017).
Kendrick, R., Chotewutmontri, P., Belcher, S. & Barkan, A. Correlated retrograde and developmental regulons implicate multiple retrograde signals as coordinators of chloroplast development in maize. Plant Cell 34, 4897–4919 (2022).
Barkan, A. Nuclear Mutants of Maize with Defects in Chloroplast Polysome Assembly Have Altered Chloroplast RNA Metabolism. Plant Cell 5, 389 (1993).
Nishimura, K., Ashida, H., Ogawa, T. & Yokota, A. A DEAD box protein is required for formation of a hidden break in Arabidopsis chloroplast 23S rRNA. Plant J. 63, 766–777 (2010).
Tiller, N. et al. The plastid-specific ribosomal proteins of Arabidopsis thaliana can be divided into non-essential proteins and genuine ribosomal proteins. Plant J. 69, 302–316 (2012).
Liu, X. et al. Genetic interactions reveal that specific defects of chloroplast translation are associated with the suppression of var2-mediated leaf variegation. J. Integr. Plant Biol. 55, 979–993 (2013).
De Longevialle, F. et al. The pentatricopeptide repeat gene OTP51 with two LAGLIDADG motifs is required for the cis -splicing of plastid ycf3 intron 2 in Arabidopsis thaliana. Plant J. 56, 157–168 (2008).
Wang, C. et al. Rerouting of ribosomal proteins into splicing in plant organelles. Proc. Natl. Acad. Sci. USA 117, 29979–29987 (2020).
Roy, S., Ueda, M., Kadowaki, K. I. & Tsutsumi, N. Different status of the gene for ribosomal protein S16 inthe chloroplast genome during evolution of the genus Arabidopsis and closely related species. Genes Genet. Syst. 85, 319–326 (2010).
Ruf, S. et al. Reverse genetics in the Arabidopsis chloroplast genome identifies rps16 as a transcribed pseudogene. Plant J. 122, e70198 (2025).
Zhang, J. et al. Arabidopsis thaliana branching enzyme 1 is essential for amylopectin biosynthesis and cesium tolerance. J. Plant Physiol. 252, 153208 (2020).
Anderson, B. M., Krause, K. & Petersen, G. Mitochondrial genomes of two parasitic Cuscuta species lack clear evidence of horizontal gene transfer and retain unusually fragmented ccmFC genes. BMC Genom. 22, 1–17 (2021).
Grimaud, F., Rogniaux, H., James, M. G., Myers, A. M. & Planchot, V. Proteome and phosphoproteome analysis of starch granule-associated proteins from normal maize and mutants affected in starch biosynthesis. J. Exp. Bot. 59, 3395–3406 (2008).
Helle, S. et al. Proteome Analysis of Potato Starch Reveals the Presence of New Starch Metabolic Proteins as Well as Multiple Protease Inhibitors. Front. Plant Sci. 9, 1–14 (2018).
Majeran, W. et al. Nucleoid-enriched proteomes in developing plastids and chloroplasts from maize leaves: A new conceptual framework for nucleoid functions. Plant Physiol. 158, 156–189 (2011).
Huang, M. et al. Construction of plastid reference proteomes for maize and Arabidopsis and evaluation of their orthologous relationships; The concept of orthoproteomics. J. Proteome Res. 12, 491–504 (2013).
Powikrowska, M., Oetke, S., Jensen, P. E. & Krupinska, K. Dynamic composition, shaping and organization of plastid nucleoids. Front. Plant Sci. 5, 1–13 (2014).
Hayashi, M. et al. Bound substrate in the structure of cyanobacterial branching enzyme supports a new mechanistic model. J. Biol. Chem. 292, 5465–5475 (2017).
Perron, K., Goldschmidt-Clermont, M. & Rochaix, J. D. A factor related to pseudouridine synthases is required for chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii. EMBO J. 18, 6481–6490 (1999).
Jenkins, B. D. & Barkan, A. Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts. EMBO J. 20, 872–879 (2001).
Liere, K. & Link, G. RNA-binding activity of the matK protein encoded by the chloroplast trnk intron from mustard (Sinapis alba L.). Nucleic Acids Res 23, 917–921 (1995).
Paukstelis, P. J., Chen, J., Chase, E., Lambowitz, A. M. & Golden, B. L. Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA. Nature 451, 94–98 (2008).
Rho, S. B., Lincecum, T. L. & Martinis, S. A. An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing. EMBO J. 21, 6874–6881 (2002).
Diesh, C. et al. JBrowse 2: a modular genome browser with views of synteny and structural variation. Genome Biol. 24, 74 (2023).
Grefen, C. et al. A ubiquitin-10 promoter-based vector set for fluorescent protein tagging facilitates temporal stability and native protein distribution in transient and stable expression studies. Plant J. 64, 355–365 (2010).
Siligato, R. et al. Multisite gateway-compatible cell type-specific gene-inducible system for plants. Plant Physiol. 170, 627–641 (2016).
Abt, M. R. et al. STARCH SYNTHASE5, a noncanonical starch synthase-like protein, promotes starch granule initiation in Arabidopsis. Plant Cell 32, 2543–2565 (2020).
Chambers, M. C. et al. A cross-platform toolkit for mass spectrometry and proteomics. Nat. Biotechnol. 30, 918–920 (2012).
Yu, F. et al. Analysis of DIA proteomics data using MSFragger-DIA and FragPipe computational platform. Nat. Commun. 14, 1–14 (2023).
Demichev, V., Messner, C. B., Vernardis, S. I., Lilley, K. S. & Ralser, M. DIA-NN: neural networks and interference correction enable deep proteome coverage in high throughput. Nat. Methods 17, 41–44 (2020).
Kong, A. T., Leprevost, F. V., Avtonomov, D. M., Mellacheruvu, D. & Nesvizhskii, A. I. MSFragger: Ultrafast and comprehensive peptide identification in mass spectrometry-based proteomics. Nat. Methods 14, 513–520 (2017).
Didusch, S., Madern, M., Hartl, M. & Baccarini, M. Amica: an Interactive and user-friendly web-platform for the analysis of proteomics data. BMC Genomics 23, 1–9 (2022).
Ritchie, M. E. et al. Limma powers differential expression analyses for RNA-sequencing and microarray studies. Nucleic Acids Res 43, e47 (2015).
Thomas, P. D. et al. PANTHER: Making genome-scale phylogenetics accessible to all. Protein Science 31, 8–22 (2022).
Hooper, C. M., Castleden, I. R., Tanz, S. K., Aryamanesh, N. & Millar, A. H. SUBA4: The interactive data analysis centre for Arabidopsis subcellular protein locations. Nucleic Acids Res 45, D1064–D1074 (2017).
Scarpin, M. R. et al. An updated nomenclature for plant ribosomal protein genes. Plant Cell. 35, 640–643 (2023).
Yilmazer, I. et al. Determining Protein-Protein Interaction with GFP-Trap Beads. Methods Mol. Biol. 2564, 317–323 (2023).
Voinnet, O., Rivas, S., Mestre, P. & Baulcombe, D. Retracted: An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus. Plant J. 33, 949–956 (2003).
Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367–1372 (2008).
da Veiga Leprevost, F. et al. Philosopher: a versatile toolkit for shotgun proteomics data analysis. Nat. Methods 17, 869–870 (2020).
Yu, F., Haynes, S. E. & Nesvizhskii, A. I. IonQuant enables accurate and sensitive label-free quantification with FDR-controlled match-between-runs. Mol. Cell. Proteom. 20, 100077 (2021).
Wessel, D. & Flügge, U. I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141–143 (1984).
Barkan, A. Genome-wide analysis of RNA–protein interactions in plants. Methods Mol Biol. 553, 13–37 (2009).
Ting, M. K. Y. et al. Optimization of ribosome profiling in plants including structural analysis of rRNA fragments. Plant Methods 20, 143 (2024).
Liehrmann, A. et al. DiffSegR: an RNA-seq data driven method for differential expression analysis using changepoint detection. NAR Genom. Bioinform. 5, 1–12 (2023).
Cannone, J. J. et al. The comparative RNA Web (CRW) site: an online database of comparative sequence and structure information for ribosomal, intron, and other RNAs. BMC Bioinform. 3, 1–31 (2002).
Kindgren, P. et al. The plastid redox insensitive 2 mutant of Arabidopsis is impaired in PEP activity and high light-dependent plastid redox signalling to the nucleus. Plant J. 70, 279–291 (2012).
Devers, E. A. et al. Movement and differential consumption of short interfering RNA duplexes underlie mobile RNA interference. Nat. Plants 6, 789–799 (2020).
Reiter, B. et al. The Arabidopsis protein CGL20 is required for plastid 50S ribosome biogenesis. Plant Physiol. 182, 1222–1238 (2020).
Lee, M. E., DeLoache, W. C., Cervantes, B. & Dueber, J. E. A highly characterized yeast toolkit for modular, multipart assembly. ACS Synth. Biol. 4, 975–986 (2015).
Mikkelsen, M. D. et al. Microbial production of indolylglucosinolate through engineering of a multi-gene pathway in a versatile yeast expression platform. Metab. Eng. 14, 104–111 (2012).
Rodrigues, N. F., Christoff, A. P., da Fonseca, G. C., Kulcheski, F. R. & Margis, R. Unveiling Chloroplast RNA Editing Events Using Next Generation Small RNA Sequencing Data. Front. Plant Sci. 8, 1686 (2017).
Katoh, K., Rozewicki, J. & Yamada, K. D. MAFFT online service: Multiple sequence alignment, interactive sequence choice and visualization. Brief. Bioinform. 20, 1160–1166 (2018).
Letunic, I. & Bork, P. Interactive Tree of Life (iTOL) v6: recent updates to the phylogenetic tree display and annotation tool. Nucleic Acids Res 52, 78–82 (2024).
Crooks, G. E., Hon, G., Chandonia, J. M. & Brenner, S. E. WebLogo: A sequence logo generator. Genome Res 14, 1188–1190 (2004).
Letunic, I., Doerks, T. & Bork, P. SMART: recent updates, new developments and status in 2015. Nucleic Acids Res 43, D257–D260 (2014).
Paysan-Lafosse, T. et al. InterPro in 2022. Nucleic Acids Res 51, D418–D427 (2023).
Emanuelsson, O., Nielsen, H. & von Heijne, G. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8, 978–984 (1999).
Erdos, G. & Dosztányi, Z. AIUPred: Combining energy estimation with deep learning for the enhanced prediction of protein disorder. Nucleic Acids Res 52, W176–W181 (2024).
Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583–589 (2021).
Abramson, J. et al. Accurate structure prediction of biomolecular interactions with AlphaFold 3. Nature 630, 493–500 (2024).
Álvarez-Salmoral, D. et al. AlphaBridge: tools for the analysis of predicted biomolecular complexes. Preprint at https://doi.org/10.1101/2024.10.23.619601 (2024).
Pettersen, E. F. et al. UCSF ChimeraX: Structure visualization for researchers, educators, and developers. Protein Sci. 30, 70–82 (2021).
Perez-Riverol, Y. et al. The PRIDE database at 20 years: 2025 update. Nucleic Acids Res 53, D543–D553 (2025).
Clough, E. et al. NCBI GEO: archive for gene expression and epigenomics data sets: 23-year update. Nucleic Acids Res 52, D138–D144 (2024).
Acknowledgements
We thank Martha Stadler for excellent technical support, Andrea Ruckle for help with plant cultivation, Christian Schmitz-Linneweber (HU Berlin) for providing us with the NtMatK C+ and C- tobacco lines and Ari Pekka Mähönen (University of Helsinki) for providing us with the pH7m34GW vector. We thank Bernd Roschitzki, Sibylle Pfammatter, Paolo Nanni and Tobias Kockmann from the Functional Genomics Center Zurich (FGCZ) for help with the proteomics analyses. AlphaFold2 structure predictions were performed on the ETH Zurich Euler computing cluster. RT-qPCR and TapeStation data were produced in collaboration with the Genetic Diversity Centre (GDC), ETH Zurich. This project has received funding from the European Union’s Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie (MSC) grant agreement No 847585 (to S.C.Z. and B.P.) and from the Vontobel Foundation (to B.P.). R.Z. is supported by the Max Planck Society and the DFG grant ZO 302/5-1.
Funding
Open access funding provided by Swiss Federal Institute of Technology Zurich.
Author information
Authors and Affiliations
Contributions
B.P., Y.L., and S.C.Z. designed the research. Y.L. conducted most of the research. Y.G., A.F., M.A., A.G., M.G., C.L., M.S., and B.P. collected and analyzed data. Y.L. prepared the figures. B.P. and Y.L. wrote the manuscript. S.C.Z, A.G., R.Z., M.S., and Y.G. edited the manuscript. B.P., S.C.Z., and R.Z. supervised the research and acquired funding. All authors read and approved the manuscript.
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing interests.
Peer review
Peer review information
Nature Communications thanks the anonymous reviewer(s) for their contribution to the peer review of this work. A peer review file is available.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Source data
Rights and permissions
Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
About this article
Cite this article
Liang, Y., Gao, Y., Fontana, A. et al. Maturase K forms a plastidial splicing complex with a neofunctionalized branching enzyme. Nat Commun (2026). https://doi.org/10.1038/s41467-026-70734-3
Received:
Accepted:
Published:
DOI: https://doi.org/10.1038/s41467-026-70734-3
