An aromatic amino acid motif in the CD5 loop of TgCIA1 facilitates mitochondrial targeting.

(A) Sanger DNA sequencing chromatograms depicting the nucleotides modified in the TgCIA1 gene to generate substitutions of the W526, Y527, and R533 residues of the protein to alanine. Mutated codons for each line are highlighted with a magenta box. <...

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Bibliographic Details
Main Author:	Evie R. Hodgson (21866946) (author)
Other Authors:	Jenni A. Hayward (10063377) (author), Rachel A. Leonard (5195411) (author), F. Victor Makota (16625292) (author), Giel G. van Dooren (10063383) (author)
Published:	2025
Subjects:	Biochemistry Medicine Microbiology Cell Biology Immunology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Physical Sciences not elsewhere classified iron – sulfur eukaryotic cell biology elucidates pivotal differences div >< p exhibit dual localization nuclear client proteins toxoplasma gondii </ cia targeting complex toxoplasma </ nuclear proteins gondii </ mitochondrial targeting three proteins study provides showed previously scaffold protein remained unclear present evidence otherwise ancient may reflect living relatives important group functionally conserved comprehensive analysis closest free cia1 protein
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An aromatic amino acid motif in the CD5 loop of <i>Tg</i>CIA1 facilitates mitochondrial targeting.

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