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.

Related Concept Videos

Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
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-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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 Thylakoids01:22

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...