Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum

Michael J LaGier1, Jan Tachezy2, Frantisek Stejskal3

  • 1Wadsworth Center, New York State Department of Health, PO Box 22002, Albany, NY 12201-2002, USA.

Insights

The iron-sulfur cluster assembly machinery in Cryptosporidium parvum is located in the mitochondria. This finding suggests the parasite retains its mitochondria for essential iron-sulfur cluster synthesis.

Area of Science:

  • Biochemistry
  • Parasitology
  • Cell Biology

Background:

  • Iron-sulfur [Fe-S] cluster assembly machinery is typically found in mitochondria and chloroplasts in eukaryotes.
  • Key proteins involved include cysteine desulfurase (IscS) and scaffold protein (IscU).
  • Cryptosporidium parvum is an opportunistic pathogen lacking effective treatments.

Purpose of the Study:

  • To isolate and characterize IscS and IscU homologues in Cryptosporidium parvum.
  • To investigate the cellular localization of [Fe-S] assembly machinery in this parasite.

Main Methods:

  • Gene isolation and characterization of IscS and IscU homologues from C. parvum.
  • Primary sequence analysis and phylogenetic studies of CpIscS and CpIscU.
  • In silico prediction of N-terminal signal sequences and targeting to yeast mitochondria.

Main Results:

  • Genes encoding IscS and IscU homologues (CpIscS and CpIscU) were identified in C. parvum.
  • Sequence and phylogenetic analyses indicate CpIscS and CpIscU are most similar to mitochondrial proteins.
  • In silico analysis predicted signal sequences targeting CpIscS and CpIscU to mitochondria.

Conclusions:

  • The findings suggest that C. parvum retains its mitochondrial relict for iron-sulfur cluster assembly.
  • This localization is crucial for the parasite's survival and pathogenesis.
  • Understanding this pathway could lead to new therapeutic strategies against C. parvum infections.

Related Concept Videos

Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
Fungal Phylum Microsporidia01:28

Fungal Phylum Microsporidia

Microsporidia are a group of obligate intracellular fungi that were initially classified as protists but were later reclassified based on phylogenetic, molecular, and structural evidence linking them to the Chytridiomycota. These unicellular, non-motile organisms are highly specialized parasites that infect a wide range of animal hosts, including humans. They have evolved extensive genomic and metabolic reductions, making them highly dependent on their hosts for survival.Morphology and Genomic...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
Diversity of Protists II01:27

Diversity of Protists II

Alveolates are a group of organisms recognized by the presence of alveoli, which are cytoplasmic sacs located beneath the cell membrane. While their function remains uncertain, alveoli may help regulate water balance by controlling how much water enters and leaves the cell. In dinoflagellates, these structures may serve as armor plates. There are three major types of alveolates: ciliates, which move using cilia; dinoflagellates, which use flagella for movement; and apicomplexans, which are...
Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...