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Subcellular multitasking – multiple destinations and roles for the Plasmodium falcilysin protease
Author(s) -
Ralph Stuart A.
Publication year - 2007
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05528.x
Subject(s) - biology , protease , plasmodium (life cycle) , subcellular localization , plastid , vacuole , microbiology and biotechnology , gene , compartment (ship) , computational biology , genetics , biochemistry , cytoplasm , enzyme , parasite hosting , oceanography , chloroplast , world wide web , computer science , geology
Summary The Plasmodium falcilysin protease is a M16‐family protease that has been previously identified as a food vacuole enzyme that participates in the breakdown of haemoglobin. Plant homologues of this protease are responsible for breaking down transit peptides that have been processed in mitochondria and plastids, and in this issue of Molecular Microbiology , Ponpuak and colleagues show that falcilysin participates in degradation of transit peptides and haemoglobin in discrete subcellular organelles. The recruitment of a gene product from one cellular compartment to another is a recurring phenomenon in molecular evolutionary biology, and arises through a number of distinct mechanisms. Plasmodium accomplishes this triple act by targeting products of the single falcilysin gene to multiple compartments.