NDLI: Plasmodium falciparum Apicoplast Transit Peptides are Unstructured in vitro and During Apicoplast Import

Content Provider	PubMed Central
Author	Gallagher, John R. Matthews, Krista A. Prigge, Sean T.
Copyright Year	2011
Abstract	Trafficking of soluble proteins to the apicoplast in Plasmodium falciparum is determined by an N-terminal transit peptide (TP) which is necessary and sufficient for apicoplast import. Apicoplast precursor proteins are synthesized at the rough endoplasmic reticulum, but are then specifically sorted from other proteins in the secretory pathway. The mechanism of TP recognition is presently unknown. Apicoplast TPs do not contain a conserved sequence motif; therefore, we asked whether they contain an essential structural motif. Using nuclear magnetic resonance to study a model TP from acyl carrier protein, we found a short, low-occupancy helix, but the TP was otherwise disordered. Using an in vivo localization assay, we blocked TP secondary structure by proline mutagenesis, but found robust apicoplast localization. Alternatively, we increased the helical content of the TP through mutation while maintaining established TP characteristics. Apicoplast import was disrupted in a helical mutant TP, but import was then restored by the further addition of a single proline. We conclude that structure in the TP interferes with apicoplast import, and therefore TPs are functionally disordered. These results provide an explanation for the amino acid bias observed in apicoplast TPs.
Related Links	http://dx.doi.org/10.1111/j.1600-0854.2011.01232.x
Ending Page	1138
Page Count	15
Starting Page	1124
File Format	PDF
ISSN	13989219
e-ISSN	16000854
Journal	Traffic (Copenhagen, Denmark)
Issue Number	9
Volume Number	12
Language	English
Publisher Date	2011-09-01
Access Restriction	Open
Subject Keyword	Genetics Cell Biology Biochemistry Molecular Biology Structural Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Genetics Structural Biology Molecular Biology Biochemistry

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