An Organellar Maturase Associates with Multiple Group II Introns

Bacterial group II introns encode maturase proteins required for splicing. In organelles of photosynthetic land plants, most of the group II introns have lost the reading frames for maturases. Here, we show that the plastidial maturase MatK not only interacts with its encoding intron within trnk-UUU...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 107; no. 7; pp. 3245 - 3250
Main Authors Zoschke, Reimo, Nakamura, Masayuki, Liere, Karsten, Sugiura, Masahiro, Börner, Thomas, Schmitz-Iinneweber, Christian, Lambowitz, Alan M.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 16.02.2010
National Acad Sciences
Subjects
Base Sequence
Binding sites
Biological Sciences
Blotting, Western
Cells
Chloroplasts
Chloroplasts - genetics
Cloning, Molecular
Deoxyribonucleic acid
DNA
Endoribonucleases - genetics
Evolution, Molecular
Flowers & plants
Gene expression
Genes
Genetic vectors
Genetic Vectors - genetics
Genomes
Immunoprecipitation
Introns
Introns - genetics
Introns - physiology
Language
Mapping
Molecular Sequence Data
Nicotiana - genetics
Nucleotidyltransferases - genetics
Organelles
Plant cells
Plants
Plastids
Proteins
RNA
RNA Splicing - genetics
RNA Splicing - physiology
RNA, Catalytic - genetics
RNA, Catalytic - physiology
Spliceosomes - genetics
Splicing
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Summary:Bacterial group II introns encode maturase proteins required for splicing. In organelles of photosynthetic land plants, most of the group II introns have lost the reading frames for maturases. Here, we show that the plastidial maturase MatK not only interacts with its encoding intron within trnk-UUU, but also with six additional group II introns, all belonging to intron subclass llA. Mapping analyses of RNA binding sites revealed MatK to recognize multiple regions within the trnK intron. Organellar group ll introns are considered to be the ancestors of nuclear spliceosomal introns. That MatK associates with multiple intron ligands makes it an attractive model for an early trans-acting nuclear splicing activity.
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Edited by Alan M. Lambowitz, The University of Texas at Austin, Austin, TX, and approved December 18, 2009 (received for review August 19, 2009)
Author contributions: R.Z., M.S., T.B., and C.S.-L. designed research; R.Z. and M.N. performed research; R.Z., M.N., K.L., and C.S.-L. analyzed data; and C.S.-L. wrote the paper.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0909400107