Related Experiment Video
Updated: Aug 24, 2026

Preparation of Intact Tissue for Microscopic Analysis of the Endosperm Cell Layer in Developing and Mature Arabidopsis Seeds
Published on: May 16, 2025
AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis
Xiang Ming Xu1, Simon Geir Møller
1Department of Biology, University of Leicester, Leicester LE1 7RH, United Kingdom.
Insights
Iron-sulfur cluster assembly is crucial for plant development. A specific protein, AtNAP7, is essential for Arabidopsis embryogenesis, highlighting the importance of plastid iron-sulfur cluster maintenance.
Area of Science:
- Plant Biology
- Biochemistry
- Molecular Biology
Background:
- Iron-sulfur (Fe-S) clusters are vital cofactors in numerous cellular processes across all domains of life.
- Defects in Fe-S cluster availability cause human diseases, underscoring their importance.
- While Fe-S proteins are crucial in plants, their biogenesis and the consequences of assembly defects remain largely unknown.
Purpose of the Study:
- To investigate the role of iron-sulfur cluster biogenesis in plant development, specifically focusing on the SufC homolog AtNAP7 in Arabidopsis thaliana.
- To elucidate the function and localization of AtNAP7 and its contribution to Fe-S cluster homeostasis during embryogenesis.
Main Methods:
- Generated Arabidopsis mutants deficient in the AtNAP7 gene.
- Analyzed embryo lethality and developmental defects.
- Determined AtNAP7 localization using microscopy.
- Assessed the ability of AtNAP7 to rescue bacterial mutants under oxidative stress.
- Investigated protein interactions between AtNAP7 and other SUF system components.
Main Results:
- Arabidopsis plants lacking AtNAP7 exhibited lethality at the globular stage of embryogenesis.
- AtNAP7 is expressed in key developmental tissues, including meristems and developing embryos.
- AtNAP7 is localized to plastids and can functionally complement an E. coli SufC mutant.
- Mutant embryos displayed abnormal plastid development with disorganized thylakoids.
- AtNAP7 interacts with AtNAP6 (a SufD homolog), suggesting a functional SUF system within Arabidopsis plastids.
Conclusions:
- AtNAP7 is a conserved SufC protein essential for iron-sulfur cluster biogenesis and/or repair in plants.
- Plastidic iron-sulfur cluster maintenance is critical for successful Arabidopsis embryogenesis.
- The SUF system likely operates within Arabidopsis plastids to ensure Fe-S cluster homeostasis.
Abstract:
In bacteria, yeast, and mammals, iron-sulfur (Fe-S) cluster-containing proteins are involved in numerous processes including electron transfer, metabolic reactions, sensing, signaling, and regulation of gene expression. In humans, iron-storage diseases such as X-linked sideroblastic anemia and ataxia are caused by defects in Fe-S cluster availability. The biogenesis of Fe-S clusters involves several pathways, and in bacteria, the SufABCDSE operon has been shown to play a vital role in Fe-S biogenesis and repair during oxidative stress. Although Fe-S proteins play vital roles in plants, Fe-S cluster biogenesis and maintenance and physiological consequences of dysfunctional Fe-S cluster assembly remains obscure. Here we report that Arabidopsis plants deficient for the SufC homolog AtNAP7 show lethality at the globular stage of embryogenesis. AtNAP7 is expressed in developing embryos and in apical, root, and floral meristems and encodes an ATP-binding cassette/ATPase that can partially rescue growth defects in an Escherichia coli SufC mutant during oxidative stress. AtNAP7 is plastid-localized, and mutant embryos contain abnormal developing plastids with disorganized thylakoid structures. We found that AtNAP7 can interact with AtNAP6, a plastidic Arabidopsis SufD homolog, and because Arabidopsis plastids also harbor SufA, SufB, SufS, and SufE homologs, plastids probably contain a complete SUF system. Our results imply that AtNAP7 represents a conserved SufC protein involved in the biogenesis and/or repair of oxidatively damaged Fe-S clusters and suggest an important role for plastidic Fe-S cluster maintenance and repair during Arabidopsis embryogenesis.
Related Concept Videos
Protein Transport to the Inner Chloroplast Membrane
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Protein Transport to the Thylakoids
ATP Synthase: Mechanism
ATP Synthase: Structure

