Plant Molecular Biology

, Volume 93, Issue 4–5, pp 355–368

The PPR protein SLOW GROWTH 4 is involved in editing of nad4 and affects the splicing of nad2 intron 1


DOI: 10.1007/s11103-016-0566-4

Cite this article as:
Weißenberger, S., Soll, J. & Carrie, C. Plant Mol Biol (2017) 93: 355. doi:10.1007/s11103-016-0566-4


Key message

SLO4 is a mitochondrial PPR protein that is involved in editing nad4, possibly required for the efficient splicing of nad2 intron1.


Pentatricopeptide repeat (PPR) proteins constitute a large protein family in flowering plants and are thought to be mostly involved in organellar RNA metabolism. The subgroup of PLS-type PPR proteins were found to be the main specificity factors of cytidine to uridine RNA editing. Identifying the targets of PLS-type PPR proteins can help in elucidating the molecular function of proteins encoded in the organellar genomes. In this study, plants lacking the SLOW GROWTH 4 PPR protein were characterized. Slo4 mutants were characterized as having restricted root growth, being late flowering and displaying an overall delayed growth phenotype. Protein levels and activity of mitochondrial complex I were decreased and putative complex I assembly intermediates accumulated in the mutant plants. An editing defect, leading to an amino acid change, in the mitochondrial nad4 transcript, encoding for a complex I subunit, was identified. Furthermore, the splicing efficiency of the first intron of nad2, encoding for another complex I subunit, was also decreased. The change in splicing efficiency could however not be linked to any editing defects in the nad2 transcript.


Mitochondria Complex I RNA editing Splicing Pentatricopeptide repeat 

Supplementary material

11103_2016_566_MOESM1_ESM.pdf (51 kb)
Supplementary material 1 (PDF 51 KB)
11103_2016_566_MOESM2_ESM.pdf (1.2 mb)
Supplementary material 2 (PDF 1181 KB)
11103_2016_566_MOESM3_ESM.pdf (6 mb)
Supplementary material 3 (PDF 6142 KB)
11103_2016_566_MOESM4_ESM.pdf (71 kb)
Supplementary material 4 (PDF 70 KB)
11103_2016_566_MOESM5_ESM.pdf (45 kb)
Supplementary material 5 (PDF 45 KB)

Funding information

Funder NameGrant NumberFunding Note
Deutsche Forschungsgemeinschaft

    Copyright information

    © Springer Science+Business Media Dordrecht 2016

    Authors and Affiliations

    1. 1.Department of Biology IBotany, Ludwig-Maximilians-Universität MünchenPlanegg-MartinsriedGermany
    2. 2.Munich Center for Integrated Protein ScienceCiPSM, Ludwig-Maximilians-Universität MünchenMunichGermany

    Personalised recommendations