AtMBP-1, an alternative translation product of LOS2, affects abscisic acid responses and is modulated by the E3 ubiquitin ligase AtSAP5

Authors

  • Miyoung Kang,

    1. Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK, USA
    2. Institute for Agricultural Bioscience, Oklahoma State University, Ardmore, OK, USA
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  • Haggag Abdelmageed,

    1. Institute for Agricultural Bioscience, Oklahoma State University, Ardmore, OK, USA
    2. Department of Agricultural Botany, Faculty of Agriculture, Cairo University, Giza, Egypt
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  • Seonghee Lee,

    1. Plant Biology Division, The Samuel Roberts Noble Foundation, Ardmore, OK, USA
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  • Angelika Reichert,

    1. Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK, USA
    2. Institute for Agricultural Bioscience, Oklahoma State University, Ardmore, OK, USA
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  • Kirankumar S. Mysore,

    1. Plant Biology Division, The Samuel Roberts Noble Foundation, Ardmore, OK, USA
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  • Randy D. Allen

    Corresponding author
    1. Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK, USA
    2. Institute for Agricultural Bioscience, Oklahoma State University, Ardmore, OK, USA
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Summary

The LOS2 gene in Arabidopsis encodes an enolase with 72% amino acid sequence identity with human ENO1. In mammalian cells, the α-enolase (ENO1) gene encodes both a 48 kDa glycolytic enzyme and a 37 kDa transcriptional suppressor protein that are targeted to different cellular compartments. The tumor suppressor c-myc binding protein (MBP-1), which is alternatively translated from the second start codon of ENO1 transcripts, is preferentially localized in nuclei while α-enolase is found in the cytoplasm. We report here that an Arabidopsis MBP-1-like protein (AtMBP-1) is alternatively translated from full-length LOS2 transcripts using a second start codon. Like mammalian MBP-1, this truncated form of LOS2 has little, if any, enolase activity, indicating that an intact N-terminal region of LOS2 is critical for catalysis. AtMBP-1 has a short half-life in vivo and is stabilized by the proteasome inhibitor MG132, indicating that it is degraded via the ubiquitin-dependent proteasome pathway. Arabidopsis plants that over-express AtMBP-1 are hypersensitive to abscisic acid (ABA) during seed germination and show defects in vegetative growth and lateral stem development. AtMBP-1 interacts directly with the E3 ubiquitin ligase AtSAP5 and co-expression of these proteins resulted in destabilization of AtMBP-1 in vivo and abolished the developmental defects associated with AtMBP-1 over-expression. Thus, AtMBP-1 is as a bona fide alternative translation product of LOS2. Accumulation of this factor is limited by ubiquitin-dependent destabilization, apparently mediated by AtSAP5.

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