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Mol. Cells 2007; 23(2): 161-169

Published online January 1, 1970

© The Korean Society for Molecular and Cellular Biology

Molecular and Functional Characterization of Monocot-specific Pex5p Splicing Variants, Using OsPex5pL and OsPex5pS from Rice (Oryza sativa)

Jung Ro Lee, Ji Hyun Jung, Jae Sook Kang, Jong Cheol Kim, In Jung Jung, Min Sook Seok, Ji Hye Kim, Woe Yeon Kim, Min Gab Kim, Jae-Yean Kim, Chae Oh Lim, Kyun Oh Lee, Sang Yeol Lee

Abstract

We identified two alternatively spliced variants of the peroxisomal targeting signal 1 (PTS1) receptor protein Pex5ps in monocot (rice, wheat, and barley) but not in dicot (Arabidopsis and tobacco) plants. We characterized the molecular and functional differences between the rice (Oryza sativa) Pex5 splicing variants OsPex5pL and OsPex5pS. There is only a single-copy of OsPEX5 in the rice genome and RT-PCR analysis points to alternative splicing of the transcripts. Putative light-responsive cis-elements were identified in the 5? region flanking OsPEX5L and Northern blot analysis demonstrated that this region affected light-dependent expression of OsPEX5 transcription. Using the pex5-deficient yeast mutant Scpex5, we showed that OsPex5pL and OsPex5pS are able to restore translocation of a model PTS1 protein (GFP-SKL) into peroxisomes. OsPex5pL and OsPex5pS formed homo-complexes via specific interaction domains, and interacted with each other and OsPex14p to form hetero-complexes. Although overexpression of OsPex5pL in the Arabidopsis pex5 mutant (Atpex5) rescued the mutant phenotype, overexpression of OsPex5pS only resulted in partial recovery.

Keywords β-Oxidation; Alternatively Spliced Variants;, Dicot; Light-dependent Expression; Monocot; OsPex5pL;, OsPex5pS; Peroxisomal Targeting Signal 1 (PTS1)

Article

Research Article

Mol. Cells 2007; 23(2): 161-169

Published online April 30, 2007

Copyright © The Korean Society for Molecular and Cellular Biology.

Molecular and Functional Characterization of Monocot-specific Pex5p Splicing Variants, Using OsPex5pL and OsPex5pS from Rice (Oryza sativa)

Jung Ro Lee, Ji Hyun Jung, Jae Sook Kang, Jong Cheol Kim, In Jung Jung, Min Sook Seok, Ji Hye Kim, Woe Yeon Kim, Min Gab Kim, Jae-Yean Kim, Chae Oh Lim, Kyun Oh Lee, Sang Yeol Lee

Abstract

We identified two alternatively spliced variants of the peroxisomal targeting signal 1 (PTS1) receptor protein Pex5ps in monocot (rice, wheat, and barley) but not in dicot (Arabidopsis and tobacco) plants. We characterized the molecular and functional differences between the rice (Oryza sativa) Pex5 splicing variants OsPex5pL and OsPex5pS. There is only a single-copy of OsPEX5 in the rice genome and RT-PCR analysis points to alternative splicing of the transcripts. Putative light-responsive cis-elements were identified in the 5? region flanking OsPEX5L and Northern blot analysis demonstrated that this region affected light-dependent expression of OsPEX5 transcription. Using the pex5-deficient yeast mutant Scpex5, we showed that OsPex5pL and OsPex5pS are able to restore translocation of a model PTS1 protein (GFP-SKL) into peroxisomes. OsPex5pL and OsPex5pS formed homo-complexes via specific interaction domains, and interacted with each other and OsPex14p to form hetero-complexes. Although overexpression of OsPex5pL in the Arabidopsis pex5 mutant (Atpex5) rescued the mutant phenotype, overexpression of OsPex5pS only resulted in partial recovery.

Keywords: β-Oxidation, Alternatively Spliced Variants,, Dicot, Light-dependent Expression, Monocot, OsPex5pL,, OsPex5pS, Peroxisomal Targeting Signal 1 (PTS1)

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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