DEAD‐box RNA helicases in <i>Arabidopsis thaliana</i>: establishing a link between quantitative expression, gene structure and evolution of a family of genes

Mingam, Annaïck; Toffano‐Nioche, Claire; Brunaud, Véronique; Boudet, Nathalie; Kreis, Martin E.; Lecharny, Alain

doi:10.1111/j.1467-7652.2004.00084.x

Cited by 65 publications

(52 citation statements)

References 77 publications

(82 reference statements)

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“…ISE1 (At1g12770) encodes a highly conserved 441-aa DEAD-box RNA helicase domain and a unique 110-aa N-terminal domain. ISE1 was described previously as RNA helicase 47 (16). ISE1 has all highly conserved motifs necessary for the RNA helicase function of DEAD-box proteins (17) (Fig.…”

Section: Resultsmentioning

confidence: 99%

Loss of the plant DEAD-box protein ISE1 leads to defective mitochondria and increased cell-to-cell transport via plasmodesmata

Stonebloom

Burch‐Smith²,

Kim³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

137

120

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Plants have intercellular channels, plasmodesmata (PD), that span the cell wall to enable cell-to-cell transport of micro-and macromolecules. We identified an Arabidopsis thaliana embryo lethal mutant increased size exclusion limit 1 (ise1) that results in increased PDmediated transport of fluorescent tracers. The ise1 mutants have a higher frequency of branched and twinned PD than wild-type embryos. Silencing of ISE1 in mature Nicotiana benthamiana leaves also leads to increased PD transport, as monitored by intercellular movement of a GFP fusion to the tobacco mosaic virus movement protein.ISE1 encodes a putative plant-specific DEAD-box RNA helicase that localizes specifically to mitochondria. The N-terminal 100 aa of ISE1 specify mitochondrial targeting. Mitochondrial metabolism is compromised severely in ise1 mutant embryos, because their mitochondrial proton gradient is disrupted and reactive oxygen species production is increased. Although mitochondria are essential for numerous cell-autonomous functions, the present studies demonstrate that mitochondrial function also regulates the critical cell non-cell-autonomous function of PD.intercellular ͉ traffic ͉ Arabidopsis ͉ embryogenesis ͉ Redox

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Section: Resultsmentioning

confidence: 99%

Loss of the plant DEAD-box protein ISE1 leads to defective mitochondria and increased cell-to-cell transport via plasmodesmata

Stonebloom

Burch‐Smith²,

Kim³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

137

120

View full text Add to dashboard Cite

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“…There are 58 DEAD box proteins in Arabidopsis, most of which belong to the sf2 family, a family that is divided into DEAD, DEAH, and DExD/H subfamilies (Boudet et al, 2001;Mingam et al, 2004). The abo6 mutation Gly-334 to Glu-334 occurs in the DEXH region.…”

Section: Abo6 Encodes a Dexh Rna Helicase That Is Localized To Mitochmentioning

confidence: 99%

DEXH Box RNA Helicase–Mediated Mitochondrial Reactive Oxygen Species Production in Arabidopsis Mediates Crosstalk between Abscisic Acid and Auxin Signaling

et al. 2012

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It is well known that abscisic acid (ABA) promotes reactive oxygen species (ROS) production through plasma membraneassociated NADPH oxidases during ABA signaling. However, whether ROS from organelles can act as second messengers in ABA signaling is largely unknown. Here, we identified an ABA overly sensitive mutant, abo6, in a genetic screen for ABAmediated inhibition of primary root growth. ABO6 encodes a DEXH box RNA helicase that is involved in regulating the splicing of several genes of complex I in mitochondria. The abo6 mutant accumulated more ROS in mitochondria, as established using a mitochondrial superoxide indicator, circularly permuted yellow fluorescent protein. Two dominant-negative mutations in ABA insensitive1 (abi1-1) and abi2-1 greatly reduced ROS production in mitochondria. The ABA sensitivity of abo6 can also be compromised by the atrbohF mutation. ABA-mediated inhibition of seed germination and primary root growth in abo6 was released by the addition of reduced GSH and exogenous auxin to the medium. Expression of auxin-responsive markers ProDR5:GUS (for synthetic auxin response element D1-4 with site-directed mutants in the 59-end from soybean):bglucuronidase) and Indole-3-acetic acid inducible2:GUS was greatly reduced by the abo6 mutation. Hence, our results provide molecular evidence for the interplay between ABA and auxin through the production of ROS from mitochondria. This interplay regulates primary root growth and seed germination in Arabidopsis thaliana.

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“…DEAD box RNA helicases are ubiquitous enzymes that participate in all aspects of RNA metabolism (7). While eukaryotes generally encode numerous DEAD box RNA helicases, 25 in yeast (8) and over 50 in Arabidopsis (9), prokaryotic genomes encode fewer members, 5 in E. coli (10) and 4 in B. subtilis (11). Structurally, RNA helicases consist of two tandem RecA-like helicase domains with N-terminal and/or C-terminal extensions that provide substrate and protein interaction domains (7).…”

Section: Importancementioning

confidence: 99%

Cyanobacterial RNA Helicase CrhR Localizes to the Thylakoid Membrane Region and Cosediments with Degradosome and Polysome Complexes in Synechocystis sp. Strain PCC 6803

et al. 2016

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The cyanobacterium Synechocystis sp. strain PCC 6803 encodes a single DEAD box RNA helicase, CrhR, whose expression is tightly autoregulated in response to cold stress. Subcellular localization and proteomic analysis results indicate that CrhR localizes to both the cytoplasmic and thylakoid membrane regions and cosediments with polysome and RNA degradosome components. Evidence is presented that either functional RNA helicase activity or a C-terminal localization signal was required for polysome but not thylakoid membrane localization. Polysome fractionation and runoff translation analysis results indicate that CrhR associates with actively translating polysomes. The data implicate a role for CrhR in translation or RNA degradation in the thylakoid region related to thylakoid biogenesis or stability, a role that is enhanced at low temperature. Furthermore, CrhR cosedimentation with polysome and RNA degradosome complexes links alteration of RNA secondary structure with a potential translation-RNA degradation complex in Synechocystis. IMPORTANCEThe interaction between mRNA translation and degradation is a major determinant controlling gene expression. Regulation of RNA function by alteration of secondary structure by RNA helicases performs crucial roles, not only in both of these processes but also in all aspects of RNA metabolism. Here, we provide evidence that the cyanobacterial RNA helicase CrhR localizes to both the cytoplasmic and thylakoid membrane regions and cosediments with actively translating polysomes and RNA degradosome components. These findings link RNA helicase alteration of RNA secondary structure with translation and RNA degradation in prokaryotic systems and contribute to the data supporting the idea of the existence of a macromolecular machine catalyzing these reactions in prokaryotic systems, an association hitherto recognized only in archaea and eukarya. C ompartmentalization of metabolic processes is crucial for cells to avoid futile cycles. While this is efficiently achieved by lipid bilayers in eukaryotic cells, this solution does not generally apply in prokaryotes. Although prokaryotes have the ability to compartmentalize using invagination of the inner cell membrane, these compartments, for example, magnetosomes, tend to perform one specific function and are not widely used (1). Prokaryotes can also form proteinaceous microcompartments in which specific reactions occur, the primary cyanobacterial example being that of carboxysomes (2). Prokaryotes do not compartmentalize routine, everyday anabolic and catabolic processes such as transcription and translation or protein and RNA decay; however, there is a growing body of evidence indicating that prokaryotes spatially confine these cellular processes (3). A prime example is the localization of the RNA degradation complex, the degradosome, to the cytoplasmic membrane (CM) in Escherichia coli (4) and Bacillus subtilis (5).The E. coli degradosome consists of RNase E, polynucleotide phosphorylase (PNPase), enolase, and the DEAD box RNA he...

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DEAD‐box RNA helicases in Arabidopsis thaliana: establishing a link between quantitative expression, gene structure and evolution of a family of genes

Cited by 65 publications

References 77 publications

Loss of the plant DEAD-box protein ISE1 leads to defective mitochondria and increased cell-to-cell transport via plasmodesmata

Loss of the plant DEAD-box protein ISE1 leads to defective mitochondria and increased cell-to-cell transport via plasmodesmata

DEXH Box RNA Helicase–Mediated Mitochondrial Reactive Oxygen Species Production in Arabidopsis Mediates Crosstalk between Abscisic Acid and Auxin Signaling

Cyanobacterial RNA Helicase CrhR Localizes to the Thylakoid Membrane Region and Cosediments with Degradosome and Polysome Complexes in Synechocystis sp. Strain PCC 6803

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