Subcellular multitasking - multiple destinations and roles for the Plasmodium falcilysin protease
- Author(s)
- Ralph, SA;
- Details
- Publication Year 2007-01,Volume 63,Issue #2,Page 309-313
- Journal Title
- MOLECULAR MICROBIOLOGY
- Publication Type
- Journal Article
- Abstract
- 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.
- Publisher
- BLACKWELL PUBLISHING
- Keywords
- FALCIPAIN CYSTEINE PROTEASES; ARABIDOPSIS-THALIANA; TARGETING PEPTIDES; MALARIA PARASITES; SECRETORY PATHWAY; FOOD VACUOLE; CHLOROPLASTS; MITOCHONDRIA; GENE; EXPRESSION
- Publisher's Version
- https://doi.org/10.1111/j.1365-2958.2006.05528.x
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2007-01-01 12:00:00