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THO 2, a core member of the THO / TREX complex, is required for micro RNA production in Arabidopsis
Author(s) -
FranciscoMangilet Anchilie G.,
Karlsson Patricia,
Kim MyungHee,
Eo Hyeon Ju,
Oh Sung Aeong,
Kim Jeong Hoe,
Kulcheski Franceli Rodrigues,
Park Soon Ki,
Manavella Pablo Andrés
Publication year - 2015
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.12874
Subject(s) - rna splicing , biogenesis , mutant , arabidopsis , biology , microbiology and biotechnology , arabidopsis thaliana , immunoprecipitation , rna , microrna , rna binding protein , nuclear export signal , genetics , gene
Summary The THO / TREX complex mediates transport of nascent mRNA s from the nucleus towards the cytoplasm in animals, and has a role in small interfering RNA ‐dependent processes in plants. Here we describe five mutant alleles of Arabidopsis thaliana THO 2 , which encodes a core subunit of the plant THO / TREX complex. tho2 mutants present strong developmental defects resembling those in plants compromised in micro RNA (mi RNA ) activity. In agreement, not only were the levels of si RNA s reduced in tho2 mutants, but also those of mature mi RNA s. As a consequence, a feedback mechanism is triggered, increasing the amount of mi RNA precursors, and finally causing accumulation of mi RNA ‐targeted mRNA s. Yeast two‐hybrid experiments and confocal microscopy showed that THO 2 does not appear to interact with any of the known mi RNA biogenesis components, but rather with the splicing machinery, implying an indirect role of THO 2 in small RNA biogenesis. Using an RNA immunoprecipitation approach, we found that THO 2 interacts with mi RNA precursors, and that tho2 mutants fail to recruit such precursors into the mi RNA ‐processing complex, explaining the reduction in mi RNA production in this mutant background. We also detected alterations in the splicing pattern of genes encoding serine/arginine‐rich proteins in tho2 mutants, supporting a previously unappreciated role of the THO / TREX complex in alternative splicing.