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Journal Article

KH domain protein RCF3 is a tissue-biased regulator of the plant miRNA biogenesis cofactor HYL1

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Karlsson,  P
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

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Christie,  MD
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons273682

Seymour,  DK
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons275180

Wang,  H
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons272723

Wang,  X
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

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Hagmann,  J
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons275182

Kulcheski,  F
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons4039

Manavella,  PA
Department Molecular Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Karlsson, P., Christie, M., Seymour, D., Wang, H., Wang, X., Hagmann, J., et al. (2015). KH domain protein RCF3 is a tissue-biased regulator of the plant miRNA biogenesis cofactor HYL1. Proceedings of the National Academy of Sciences of the United States of America, 112(45), 14096-14101. doi:10.1073/pnas.1512865112.


Cite as: https://hdl.handle.net/21.11116/0000-000A-9DE3-5
Abstract
The biogenesis of microRNAs (miRNAs), which regulate mRNA abundance through posttranscriptional silencing, comprises multiple well-orchestrated processing steps. We have identified the Arabidopsis thaliana K homology (KH) domain protein REGULATOR OF CBF GENE EXPRESSION 3 (RCF3) as a cofactor affecting miRNA biogenesis in specific plant tissues. MiRNA and miRNA-target levels were reduced in apex-enriched samples of rcf3 mutants, but not in other tissues. Mechanistically, RCF3 affects miRNA biogenesis through nuclear interactions with the phosphatases C-TERMINAL DOMAIN PHOSPHATASE-LIKE1 and 2 (CPL1 and CPL2). These interactions are essential to regulate the phosphorylation status, and thus the activity, of the double-stranded RNA binding protein and DICER-LIKE1 (DCL1) cofactor HYPONASTIC LEAVES1 (HYL1).