Journal
FEBS LETTERS
Volume 590, Issue 19, Pages 3397-3406Publisher
WILEY
DOI: 10.1002/1873-3468.12382
Keywords
ClpS; N-end rule; Plasmodium falciparum
Funding
- La Trobe University Postgraduate Research Scholarship
- Australian Research Council [DP110103936, FT0992033]
- Australian Research Council [FT0992033] Funding Source: Australian Research Council
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The N-end rule is a conserved protein degradation pathway that relates the metabolic stability of a protein to the identity of its N-terminal residue. Proteins bearing a destabilising N-terminal residue (N-degron) are recognised by specialised components of the pathway (N-recognins) and degraded by cellular proteases. In bacteria, the N-recognin ClpS is responsible for the specific recognition of proteins bearing an N-terminal destabilising residue such as leucine, phenylalanine, tyrosine or tryptophan. In this study, we show that the putative apicoplast N-recognin from Plasmodium falciparum (PfClpS), in contrast to its bacterial homologues, exhibits an expanded substrate specificity that includes recognition of the branched chain amino acid isoleucine.
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