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Title of Journal: Plant Mol Biol

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Abbravation: Plant Molecular Biology

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Springer Netherlands

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DOI

10.1007/s11771-012-1251-7

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ISSN

1573-5028

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Novel interaction between CCR4 and CAF1 in rice CC

Authors: WeiLun Chou YueLin Chung JhenCheng Fang ChungAn Lu
Publish Date: 2016/10/06
Volume: 93, Issue: 1-2, Pages: 79-96
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Abstract

Rice is an important crop in the world However little is known about rice mRNA deadenylation which is an important regulation step of gene expression at the posttranscriptional level The CCR4–NOT1 complex contains two key components CCR4 and CAF1 which are the main cytoplasmic deadenylases in eukaryotic cells In yeast and humans CCR4 can interact with CAF1 via its Nterminal LRR domain However no CCR4 protein containing Nterminal LRR motifs have been found in plants In this manuscript we demonstrate a novel pattern of interaction between OsCCR4 and OsCAF1 in the rice CCR4–NOT complex and that OsCAF1 acts as a bridge between OsCCR4 and OsNOT1 in this complex Our results revealed that the Myndlike domain at the Nterminus of rice CCR4 proteins and the PXLXP motif at the rice CAF1 Nterminus play critical roles in OsCCR4–OsCAF1 interactionDeadenylation also called polyA tail shortening is the first ratelimiting step in general cytoplasmic mRNA degradation in eukaryotic cells Carbon catabolite repressor CCR4 and CCR4associated factor CAF1 in the CCR4–NOT complex function in mRNA polyA tail shortening CCR4s contain Nterminal leucinerich repeat LRR motifs that interact with CAF1s in yeast fruit fly and mammals In silico analysis has not identified any plant CCR4 proteins that contain LRR motifs Here two rice CCR4 homologous genes OsCCR4a and OsCCR4b were identified The isolated recombinant exonuclease–endonuclease–phosphatase domain of OsCCR4a and OsCCR4b exhibited 3′–5′ exonuclease activity in vitro and point mutation of a catalytic residue in this domain disrupted the deadenylase activity Both OsCCR4a and OsCCR4b fluorescent fusion proteins were localized in the rice cytoplasm and nucleus and both associated with processing bodies via their Nterminus Binding analyses showed that OsCCR4a and OsCCR4b directly interacted with three rice CAF1 family members OsCAF1A OsCAF1G and OsCAF1H The zfMYNDlike domain at the N terminus of rice CCR4 and the PXLXP motif of rice CAF1 play critical roles in OsCCR4–OsCAF1 interaction OsCAF1 proteins but not OsCCR4 proteins can interact with the MIG4G domain of rice OsNOT1 Our studies thus reveal a hitherto undiscovered novel interaction pattern that connects OsCCR4 and OsCAF1 in the rice CCR4–NOT complexWeiLun Chou and ChungAn Lu participated in the design of the study WeiLun Chou YueLin Chung and JhenCheng Fang carried out the bioinformatics analysis gene cloning realtime RTPCR subcellular localization the yeast twohybrid and BiFC WeiLun Chou and ChungAn Lu carried out data analysis and wrote manuscript All authors read and approved the final manuscript

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