Transcriptome Sequencing Identifies SPL7-Regulated Copper Acquisition Genes FRO4/FRO5 and the Copper Dependence of Iron Homeostasis in Arabidopsis

Bernal, M. Mar; Casero, David; Singh, Vasantika; Wilson, Grandon T.; Grande, Arne V.; Yang, Huijun; Dodani, Sheel C.; Pellegrini, Matteo; Huijser, Peter; Connolly, Erin L.; Merchant, Sabeeha; Krämer, Ute

doi:10.1105/tpc.111.090431

Cited by 311 publications

(429 citation statements)

References 89 publications

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“…The Chloroplast 2010 Project identified the SALK_098173 mutant (now called psb33-1) as having a very low maximal PSII quantum yield (F v /F m ) following 3 h of photoinhibiting light (1,000 PPFD). Examination of the expression of PSB33 from transcriptome sequencing studies in Arabidopsis (Bernal et al, 2012) revealed that PSB33 had a similar transcript abundance to other auxiliary PSII subunits (Supplemental Table S1). These results led to the hypothesis that the mutant was impacted in PSII function.…”

Section: Identification Of the Psb33 Genementioning

confidence: 99%

PHOTOSYSTEM II PROTEIN33, a Protein Conserved in the Plastid Lineage, Is Associated with the Chloroplast Thylakoid Membrane and Provides Stability to Photosystem II Supercomplexes in Arabidopsis

et al. 2014

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ORCID IDs: 0000-0002-2594-509X (S.S.M.); 0000-0001-6974-9587 (R.L.L.).Photosystem II (PSII) is a multiprotein complex that catalyzes the light-driven water-splitting reactions of oxygenic photosynthesis. Light absorption by PSII leads to the production of excited states and reactive oxygen species that can cause damage to this complex. Here, we describe Arabidopsis (Arabidopsis thaliana) At1g71500, which encodes a previously uncharacterized protein that is a PSII auxiliary core protein and hence is named PHOTOSYSTEM II PROTEIN33 (PSB33). We present evidence that PSB33 functions in the maintenance of PSII-light-harvesting complex II (LHCII) supercomplex organization. PSB33 encodes a protein with a chloroplast transit peptide and one transmembrane segment. In silico analysis of PSB33 revealed a light-harvesting complexbinding motif within the transmembrane segment and a large surface-exposed head domain. Biochemical analysis of PSII complexes further indicates that PSB33 is an integral membrane protein located in the vicinity of LHCII and the PSII CP43 reaction center protein. Phenotypic characterization of mutants lacking PSB33 revealed reduced amounts of PSII-LHCII supercomplexes, very low state transition, and a lower capacity for nonphotochemical quenching, leading to increased photosensitivity in the mutant plants under light stress. Taken together, these results suggest a role for PSB33 in regulating and optimizing photosynthesis in response to changing light levels.

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Section: Identification Of the Psb33 Genementioning

confidence: 99%

PHOTOSYSTEM II PROTEIN33, a Protein Conserved in the Plastid Lineage, Is Associated with the Chloroplast Thylakoid Membrane and Provides Stability to Photosystem II Supercomplexes in Arabidopsis

et al. 2014

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“…As an example, some Fe deficiency responses are up-regulated by K, S, P or Cu deficiency in dicot plants [37,56,59,136,137]. On a reciprocal basis, it is also frequent that Fe deficiency conditions induce responses to other nutrient deficiencies.…”

Section: Crosstalk Among Fe and P Deficienciesmentioning

confidence: 99%

Similarities and Differences in the Acquisition of Fe and P by Dicot Plants

et al. 2018

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This review deals with two essential plant mineral nutrients, iron (Fe) and phosphorus (P); the acquisition of both has important environmental and economic implications. Both elements are abundant in soils but are scarcely available to plants. To prevent deficiency, dicot plants develop physiological and morphological responses in their roots to specifically acquire Fe or P. Hormones and signalling substances, like ethylene, auxin and nitric oxide (NO), are involved in the activation of nutrient-deficiency responses. The existence of common inducers suggests that they must act in conjunction with nutrient-specific signals in order to develop nutrient-specific deficiency responses. There is evidence suggesting that P-or Fe-related phloem signals could interact with ethylene and NO to confer specificity to the responses to Fe-or P-deficiency, avoiding their induction when ethylene and NO increase due to other nutrient deficiency or stress. The mechanisms responsible for such interaction are not clearly determined, and thus, the regulatory networks that allow or prevent cross talk between P and Fe deficiency responses remain obscure. Here, fragmented information is drawn together to provide a clearer overview of the mechanisms and molecular players involved in the regulation of the responses to Fe or P deficiency and their interactions.

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“…Because the most bioavailable form of Cu in soils is Cu 2+ , root uptake is most often facilitated by reduction. The ferric reductase oxidases FRO1, FRO2, FRO3, FRO4 and FRO5, expressed in Arabidopsis thaliana, seem to be involved in this process (Bernal et al, 2012;Jeong and Connolly, 2009). Cu is likely to enter the cytosol of root cells through a cell surface COPT/Ctr-family transporter.…”

Section: A Coppermentioning

confidence: 99%

Influence of Soil Chemistry and Plant Physiology in the Phytoremediation of Cu, Mn, and Zn

Pinto

Aguiar

Ferreira

2014

Critical Reviews in Plant Sciences

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Transcriptome Sequencing Identifies SPL7-Regulated Copper Acquisition Genes FRO4/FRO5 and the Copper Dependence of Iron Homeostasis in Arabidopsis

Cited by 311 publications

References 89 publications

PHOTOSYSTEM II PROTEIN33, a Protein Conserved in the Plastid Lineage, Is Associated with the Chloroplast Thylakoid Membrane and Provides Stability to Photosystem II Supercomplexes in Arabidopsis

PHOTOSYSTEM II PROTEIN33, a Protein Conserved in the Plastid Lineage, Is Associated with the Chloroplast Thylakoid Membrane and Provides Stability to Photosystem II Supercomplexes in Arabidopsis

Similarities and Differences in the Acquisition of Fe and P by Dicot Plants

Influence of Soil Chemistry and Plant Physiology in the Phytoremediation of Cu, Mn, and Zn

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