- Non-mitochondrial aconitase regulates the expression of iron-uptake genes by controlling the RNA turnover process in fission yeast
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Soo-Yeon Cho , Soo-Jin Jung , Kyoung-Dong Kim , Jung-Hye Roe
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J. Microbiol. 2021;59(12):1075-1082. Published online October 26, 2021
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DOI: https://doi.org/10.1007/s12275-021-1438-4
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Abstract
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Aconitase, a highly conserved protein across all domains of
life, functions in converting citrate to isocitrate in the tricarboxylic
acid cycle. Cytosolic aconitase is also known to act as
an iron regulatory protein in mammals, binding to the RNA
hairpin structures known as iron-responsive elements within
the untranslated regions of specific RNAs. Aconitase-2 (Aco2)
in fission yeast is a fusion protein consisting of an aconitase
and a mitochondrial ribosomal protein, bL21, residing not
only in mitochondria but also in cytosol and the nucleus. To
investigate the role of Aco2 in the nucleus and cytoplasm of
fission yeast, we analyzed the transcriptome of aco2ΔN mutant
that is deleted of nuclear localization signal (NLS). RNA
sequencing revealed that the aco2ΔN mutation caused increase
in mRNAs encoding iron uptake transporters, such as
Str1, Str3, and Shu1. The half-lives of mRNAs for these genes
were found to be significantly longer in the aco2ΔN mutant
than the wild-type strain, suggesting the role of Aco2 in mRNA
turnover. The three conserved cysteines required for the catalytic
activity of aconitase were not necessary for this role.
The UV cross-linking RNA immunoprecipitation analysis
revealed that Aco2 directly bound to the mRNAs of iron uptake
transporters. Aco2-mediated degradation of iron-uptake
mRNAs appears to utilize exoribonuclease pathway that involves
Rrp6 as evidenced by genetic interactions. These results
reveal a novel role of non-mitochondrial aconitase protein
in the mRNA turnover in fission yeast to fine-tune iron
homeostasis, independent of regulation by transcriptional
repressor Fep1.
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Citations
Citations to this article as recorded by 
- Iron-mediated post-transcriptional regulation in Toxoplasma gondii
Megan A. Sloan, Adam Scott, Dana Aghabi, Lucia Mrvova, Clare R. Harding, Dominique Soldati-Favre PLOS Pathogens.2025; 21(2): e1012857. CrossRef - The Key Enzymes of Carbon Metabolism and the Glutathione Antioxidant System Protect Yarrowia lipolytica Yeast Against pH-Induced Stress
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- [Minireview]Potential roles of condensin in genome organization and beyond in fission yeast
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Kyoung-Dong Kim
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J. Microbiol. 2021;59(5):449-459. Published online April 20, 2021
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DOI: https://doi.org/10.1007/s12275-021-1039-2
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Abstract
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The genome is highly organized hierarchically by the function
of structural maintenance of chromosomes (SMC) complex
proteins such as condensin and cohesin from bacteria
to humans. Although the roles of SMC complex proteins have
been well characterized, their specialized roles in nuclear processes
remain unclear. Condensin and cohesin have distinct
binding sites and mediate long-range and short-range genomic
associations, respectively, to form cell cycle-specific
genome organization. Condensin can be recruited to highly
expressed genes as well as dispersed repeat genetic elements,
such as Pol III-transcribed genes, LTR retrotransposon, and
rDNA repeat. In particular, mitotic transcription factors Ace2
and Ams2 recruit condensin to their target genes, forming
centromeric clustering during mitosis. Condensin is potentially
involved in various chromosomal processes such as the
mobility of chromosomes, chromosome territories, DNA reannealing,
and transcription factories. The current knowledge
of condensin in fission yeast summarized in this review can
help us understand how condensin mediates genome organization
and participates in chromosomal processes in other
organisms.
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