DEAD-box RNA helicases (DBRHs) modulate RNA secondary structure, allowing RNA molecules to adopt the conformations required for interaction with their target proteins. RH50 is a chloroplast-located DBRH that co-localizes and is co-expressed with GUN1, a central factor in chloroplast-to-nucleus signaling. When combined with mutations that impair plastid gene expression (prors1-1, prpl11-1, prps1-1, prps21-1, prps17-1 and prpl24-1), rh50 and gun1 mutations evoke similar patterns of epistatic effects. These observations, together with the synergistic growth phenotype of the double mutant rh50-1 gun1-102, suggest that RH50 and GUN1 are functionally related and that this function is associated with plastid gene expression, in particular ribosome functioning. However, rh50-1 itself is not a gun mutant, although - like gun1-102 - the rh50-1 mutation suppresses the down-regulation of nuclear genes for photosynthesis induced by the prors1-1 mutation. The RH50 protein co-migrates with ribosomal particles, and is required for efficient translation of plastid proteins. RH50 binds to transcripts of the 23S-4.5S intergenic region and, in its absence, levels of the corresponding rRNA processing intermediate are strongly increased, implying that RH50 is required for the maturation of the 23S and 4.5S rRNAs. This inference is supported by the finding that loss of RH50 renders chloroplast protein synthesis sensitive to erythromycin and exposure to cold. Based on these results, we conclude that RH50 is a plastid rRNA maturation factor.

The DEAD-box RNA helicase RH50 is a 23S-4.5S rRNA maturation factor that functionally overlaps with the plastid signaling factor GUN1 / F. Paieri, L. Tadini, N. Manavski, T. Kleine, R. Ferrari, P.A. Morandini, P. Pesaresi, J. Meurer, D. Leister. - In: PLANT PHYSIOLOGY. - ISSN 0032-0889. - 176:1(2018), pp. 634-638.

The DEAD-box RNA helicase RH50 is a 23S-4.5S rRNA maturation factor that functionally overlaps with the plastid signaling factor GUN1

L. Tadini
Membro del Collaboration Group
;
R. Ferrari
Membro del Collaboration Group
;
P.A. Morandini;P. Pesaresi
Membro del Collaboration Group
;
2018

Abstract

DEAD-box RNA helicases (DBRHs) modulate RNA secondary structure, allowing RNA molecules to adopt the conformations required for interaction with their target proteins. RH50 is a chloroplast-located DBRH that co-localizes and is co-expressed with GUN1, a central factor in chloroplast-to-nucleus signaling. When combined with mutations that impair plastid gene expression (prors1-1, prpl11-1, prps1-1, prps21-1, prps17-1 and prpl24-1), rh50 and gun1 mutations evoke similar patterns of epistatic effects. These observations, together with the synergistic growth phenotype of the double mutant rh50-1 gun1-102, suggest that RH50 and GUN1 are functionally related and that this function is associated with plastid gene expression, in particular ribosome functioning. However, rh50-1 itself is not a gun mutant, although - like gun1-102 - the rh50-1 mutation suppresses the down-regulation of nuclear genes for photosynthesis induced by the prors1-1 mutation. The RH50 protein co-migrates with ribosomal particles, and is required for efficient translation of plastid proteins. RH50 binds to transcripts of the 23S-4.5S intergenic region and, in its absence, levels of the corresponding rRNA processing intermediate are strongly increased, implying that RH50 is required for the maturation of the 23S and 4.5S rRNAs. This inference is supported by the finding that loss of RH50 renders chloroplast protein synthesis sensitive to erythromycin and exposure to cold. Based on these results, we conclude that RH50 is a plastid rRNA maturation factor.
Chloroplast, Biogenesis, Retrograde Signalling, Gene expression
Settore BIO/04 - Fisiologia Vegetale
Settore BIO/18 - Genetica
   BarPLUS: modifying canopy architecture and photosynthesis to maximize barley biomass and yield for different end-uses
   BarPLUS
   MINISTERO DELL'ISTRUZIONE E DEL MERITO
2018
14-nov-2017
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/530604
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