Format

Send to

Choose Destination
Cell. 2012 Nov 9;151(4):859-870. doi: 10.1016/j.cell.2012.09.039.

Fast-forward genetics identifies plant CPL phosphatases as regulators of miRNA processing factor HYL1.

Author information

1
Department of Molecular Biology, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
2
Center for Plant Molecular Biology (ZMBP), University of Tübingen, 72076 Tübingen, Germany.
3
Proteome Center, Interfaculty Institute for Cell Biology, University of Tübingen, 72076 Tübingen, Germany.
4
Department of Molecular Biology, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany. Electronic address: weigel@weigelworld.org.

Abstract

MicroRNAs (miRNAs) are processed from primary transcripts that contain partially self-complementary foldbacks. As in animals, the core microprocessor in plants is a Dicer protein, DICER-LIKE1 (DCL1). Processing accuracy and strand selection is greatly enhanced through the RNA binding protein HYPONASTIC LEAVES 1 (HYL1) and the zinc finger protein SERRATE (SE). We have combined a luciferase-based genetic screen with whole-genome sequencing for rapid identification of new regulators of miRNA biogenesis and action. Among the first six mutants analyzed were three alleles of C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1 (CPL1)/FIERY2 (FRY2). In the miRNA processing complex, SE functions as a scaffold to mediate CPL1 interaction with HYL1, which needs to be dephosphorylated for optimal activity. In the absence of CPL1, HYL1 dephosphorylation and hence accurate processing and strand selection from miRNA duplexes are compromised. Our findings thus define a new regulatory step in plant miRNA biogenesis.

PMID:
23141542
DOI:
10.1016/j.cell.2012.09.039
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center