Dual roles of the nuclear cap-binding complex and SERRATE in pre-mRNA splicing and microRNA processing in Arabidopsis thaliana

被引:301
作者
Laubinger, Sascha [1 ]
Sachsenberg, Tirno [1 ]
Zeller, Georg [1 ,2 ]
Busch, Wolfgang [1 ]
Lohmann, Jan U. [1 ]
Raescht, Gunnar [2 ]
Weigel, Detlef [1 ]
机构
[1] Max Planck Inst Dev Biol, Dept Mol Biol, D-72076 Tubingen, Germany
[2] Friedrich Miescher Lab, D-72076 Tubingen, Germany
关键词
D O I
10.1073/pnas.0802493105
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The processing of Arabidopsis thaliana microRNAs (miRNAs) from longer primary transcripts (pri-miRNAs) requires the activity of several proteins, including DICER-LIKE1 (DCL1), the double-stranded RNA-binding protein HYPONASTIC LEAVES1 (HYL1), and the zinc finger protein SERRATE (SE). It has been noted before that the morphological appearance of weak se mutants is reminiscent of plants with mutations in ABH1/CBP80 and CBP20, which encode the two subunits of the nuclear cap-binding complex. We report that, like SE, the cap-binding complex is necessary for proper processing of pri-miRNAs. Inactivation of either ABH1/CBP80 or CBP20 results in decreased levels of mature miRNAs accompanied by apparent stabilization of pri-miRNAs. Whole-genome tiling array analyses reveal that se, abh1/cbp80, and cbp20 mutants also share similar splicing defects, leading to the accumulation of many partially spliced transcripts. This is unlikely to be an indirect consequence of improper miRNA processing or other mRNA turnover pathways, because introns retained in se, abh1/cbp80, and cbp20 mutants are not affected by mutations in other genes required for miRNA processing or for nonsense-mediated mRNA decay. Taken together, our results uncover dual roles in splicing and miRNA processing that distinguish SE and the cap-binding complex from specialized miRNA processing factors such as DCL1 and HYL1.
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页码:8795 / 8800
页数:6
相关论文
共 64 条
[31]   Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20 [J].
Ishigaki, Y ;
Li, XJ ;
Serin, G ;
Maquat, LE .
CELL, 2001, 106 (05) :607-617
[32]   A NUCLEAR CAP-BINDING PROTEIN COMPLEX INVOLVED IN PRE-MESSENGER-RNA SPLICING [J].
IZAURRALDE, E ;
LEWIS, J ;
MCGUIGAN, C ;
JANKOWSKA, M ;
DARZYNKIEWICZ, E ;
MATTAJ, IW .
CELL, 1994, 78 (04) :657-668
[33]   A CAP-BINDING PROTEIN COMPLEX MEDIATING U SNRNA EXPORT [J].
IZAURRALDE, E ;
LEWIS, J ;
GAMBERI, C ;
JARMOLOWSKI, A ;
MCGUIGAN, C ;
MATTAJ, IW .
NATURE, 1995, 376 (6542) :709-712
[34]   Both introns and long 3′-UTRs operate as cis-acting elements to trigger nonsense-mediated decay in plants [J].
Kertesz, Sandor ;
Kerenyi, Zoltan ;
Merai, Zsuzsanna ;
Bartos, Imre ;
Palfy, Tamas ;
Barta, Endre ;
Silhavy, Daniel .
NUCLEIC ACIDS RESEARCH, 2006, 34 (21) :6147-6157
[35]   mRNA metabolism of flowering-time regulators in wild-type Arabidopsis revealed by a nuclear cap binding protein mutant, abh1 [J].
Kuhn, Josef M. ;
Breton, Ghislain ;
Schroeder, Julian I. .
PLANT JOURNAL, 2007, 50 (06) :1049-1062
[36]   The interaction between DCL1 and HYL1 is important for efficient and precise processing of pri-miRNA in plant microRNA biogenesis [J].
Kurihara, Y ;
Takashi, Y ;
Watanabe, Y .
RNA, 2006, 12 (02) :206-212
[37]   Arabidopsis micro-RNA biogenesis through Dicer-like 1 protein functions [J].
Kurihara, Y ;
Watanabe, Y .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (34) :12753-12758
[38]   The role of the cap structure in RNA processing and nuclear export [J].
Lewis, JD ;
Izaurralde, E .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 247 (02) :461-469
[39]   A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing [J].
Lewis, JD ;
Gorlich, D ;
Mattaj, IW .
NUCLEIC ACIDS RESEARCH, 1996, 24 (17) :3332-3336
[40]   A new Arabidopsis gene, FLK, encodes an RNA binding protein with K homology motifs and regulates flowering time via FLOWERING LOCUS C [J].
Lim, MH ;
Kim, J ;
Kim, YS ;
Chung, KS ;
Seo, YH ;
Lee, I ;
Kim, J ;
Hong, CB ;
Kim, HJ ;
Park, CM .
PLANT CELL, 2004, 16 (03) :731-740