A1 Refereed original research article in a scientific journal
Acclimation of Oxygenic Photosynthesis to Iron Starvation Is Controlled by the sRNA IsaR1
Authors: Georg J, Kostova G, Vuorijoki L, Schon V, Kadowaki T, Huokko T, Baumgartner D, Muller M, Klahn S, Allahverdiyeva Y, Hihara Y, Futschik ME, Aro EM, Hess WR
Publisher: CELL PRESS
Publication year: 2017
Journal: Current Biology
Journal name in source: CURRENT BIOLOGY
Journal acronym: CURR BIOL
Volume: 27
Issue: 10
First page : 1425
Last page: 1436.e7
Number of pages: 19
ISSN: 0960-9822
eISSN: 1879-0445
DOI: https://doi.org/10.1016/j.cub.2017.04.010
Abstract
Oxygenic photosynthesis crucially depends on proteins that possess Fe (2+) or Fe/S complexes as co-factors or prosthetic groups. Here, we show that the small regulatory RNA (sRNA) IsaR1 (Iron-Stress-Activated RNA 1) plays a pivotal role in acclimation to low-iron conditions. The IsaR1 regulon consists of more than 15 direct targets, including Fe (2+)-containing proteins involved in photosynthetic electron transfer, detoxification of anion radicals, citrate cycle, and tetrapyrrole biogenesis. IsaR1 is essential for maintaining physiological levels of Fe/S cluster biogenesis proteins during iron deprivation. Consequently, IsaR1 affects the acclimation of the photosynthetic apparatus to iron starvation at three levels: (1) directly, via posttranscriptional repression of gene expression; (2) indirectly, via suppression of pigment; and (3) Fe/S cluster biosynthesis. Homologs of IsaR1 are widely conserved throughout the cyanobacterial phylum. We conclude that IsaR1 is a critically important riboregulator. These findings provide a new perspective for understanding the regulation of iron homeostasis in photosynthetic organisms.
Oxygenic photosynthesis crucially depends on proteins that possess Fe (2+) or Fe/S complexes as co-factors or prosthetic groups. Here, we show that the small regulatory RNA (sRNA) IsaR1 (Iron-Stress-Activated RNA 1) plays a pivotal role in acclimation to low-iron conditions. The IsaR1 regulon consists of more than 15 direct targets, including Fe (2+)-containing proteins involved in photosynthetic electron transfer, detoxification of anion radicals, citrate cycle, and tetrapyrrole biogenesis. IsaR1 is essential for maintaining physiological levels of Fe/S cluster biogenesis proteins during iron deprivation. Consequently, IsaR1 affects the acclimation of the photosynthetic apparatus to iron starvation at three levels: (1) directly, via posttranscriptional repression of gene expression; (2) indirectly, via suppression of pigment; and (3) Fe/S cluster biosynthesis. Homologs of IsaR1 are widely conserved throughout the cyanobacterial phylum. We conclude that IsaR1 is a critically important riboregulator. These findings provide a new perspective for understanding the regulation of iron homeostasis in photosynthetic organisms.
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