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The N‐end rule adaptor protein ClpS from Plasmodium falciparum exhibits broad substrate specificity
Author(s) -
Tan Ju Lin,
Ward Linda,
Truscott Kaye N.,
Dougan David A.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12382
Subject(s) - signal transducing adaptor protein , plasmodium falciparum , biology , computational biology , chemistry , microbiology and biotechnology , malaria , immunology , signal transduction
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 ( Pf ClpS), in contrast to its bacterial homologues, exhibits an expanded substrate specificity that includes recognition of the branched chain amino acid isoleucine.