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Cytosolic Fe-S cluster assembly-deficient mutant, nar1 and nbp35 mutant seedling

ABSTRACT: Expression profiling of two-weeks-old wild type, nar1-4/- and nbp35-3/- mutant seedlings. The cytosolic Fe -S cluster assembly pathway is involved in cytosolic and nucleus Fe-S protein maturation. The nar1 mutant was identified by the screeing for abnormal transcription feature in endosperm.We performed genome-wide transcriptional profiling of weak allele nar1-4/- using microarrays to estimate whether the cytosolic Fe -S cluster assembly could affect on the transcriptional profile even in vegetative tissues. Two biological replicate were performed using two weeks seedling of wild type, nar1-4/- and nbp35-3/-. RNA was extracted using the RNeasy mini kit(QIAGEN).

ORGANISM(S): Arabidopsis thaliana

SUBMITTER: Miyuki Nakamura

PROVIDER: E-GEOD-44116 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Cytosolic Fe-S cluster assembly-deficient mutant, nar1 and nbp35 mutant seedling

Project description:Expression profiling of two-weeks-old wild type, nar1-4/- and nbp35-3/- mutant seedlings. The cytosolic Fe -S cluster assembly pathway is involved in cytosolic and nucleus Fe-S protein maturation. The nar1 mutant was identified by the screeing for abnormal transcription feature in endosperm.We performed genome-wide transcriptional profiling of weak allele nar1-4/- using microarrays to estimate whether the cytosolic Fe -S cluster assembly could affect on the transcriptional profile even in vegetative tissues.

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Iron-Regulated Assembly of the Cytosolic Iron-Sulfur Cluster Biogenesis Machinery

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Dynamic Assembly of the Cytosolic Iron-Sulfur Cluster Biogenesis Machinery Requires Iron-Sulfur Cluster Incorporation of CIAO3

Project description:Cytosolic iron-sulfur (Fe-S) cluster assembly (CIA) pathway delivers Fe-S clusters to nuclear and cytosolic Fe-S proteins involved in essential cellular functions. This delivery process is regulated by availability of iron and oxygen, but it remains unclear how CIA components orchestrate the cluster transfer under varying cellular environments. Here, we investigated the organization of CIA machinery under various conditions. We developed a targeted proteomics assay monitoring known CIA factors. Using this assay, we were able to detect NUBP1, CIAO3 and CIA substrates in immunoprecipitates of NUBP2, a component of the CIA scaffold complex. We also revealed that NUBP2 transiently associates with the CIA targeting complex (MMS19, CIAO1, CIAO2B), indicating the possible existence of CIA metabolons. We observed stronger interactions between CIAO3 and the CIA scaffold complex upon iron supplementation or low oxygen tension, while iron chelation and reactive oxygen species weaken CIAO3 interactions with CIA components. We further demonstrated that CIAO3 mutant with defective Fe-S cluster binding failed to integrate into the metabolons. However, these mutants unexpectedly exhibit stronger association with CIA substrates regardless of their reduced association with the CIA targeting complex, implicating that CIAO3 and CIA substrates may present in complexes independent of the CIA targeting complex. Together, our data suggested that CIA components potentially form metabolons whose assembly are regulated by environmental cues and require Fe-S cluster incorporation in CIAO3. These findings provided additional evidence that the CIA pathway adapts to changes in cellular environment through complex reorganization.

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Expression analysis of N. europaea (ATCC 19718) wildtype and pFur::Kan mutant grown in Fe-replete and Fe-limited media

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