TY  - JOUR
AU  - van Dooren, GG
AU  - Su, V
AU  - D'Ombrain, C
AU  - McFadden, GI
Y2  - 2014/05/21
Y1  - 2002/06/28
SN  - 0021-9258
UR  - http://hdl.handle.net/11343/26619
AB  - The plastid (apicoplast) of the malaria-causing parasite Plasmodium falciparum was derived via a secondary endosymbiotic process. As in other secondary endosymbionts, numerous genes for apicoplast proteins are located in the nucleus, and the encoded proteins are targeted to the organelle courtesy of a bipartite N-terminal extension. The first part of this leader sequence is a signal peptide that targets proteins to the secretory pathway. The second, so-called transit peptide region is required to direct proteins from the secretory pathway across the multiple membranes surrounding the apicoplast. In this paper we perform a pulse-chase experiment and N-terminal sequencing to show that the transit peptide of an apicoplast-targeted protein is cleaved, presumably upon import of the protein into the apicoplast. We identify a gene whose product likely performs this cleavage reaction, namely a stromal-processing peptidase (SPP) homologue. In plants SPP cleaves the transit peptides of plastid-targeted proteins. The P. falciparum SPP homologue contains a bipartite N-terminal apicoplast-targeting leader. Interestingly, it shares this leader sequence with a Delta-aminolevulinic acid dehydratase homologue via an alternative splicing event.
N1  - application/pdf
LA  - English
PB  - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
KW  - Infectious Agents; Infectious Diseases
T1  - Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme
DO  - 10.1074/jbc.M201748200
IS  - JOURNAL OF BIOLOGICAL CHEMISTRY
VL  - 277
IS  - 26
SP  - 23612-23619
L1  - /bitstream/handle/11343/26619/116833_5473.pdf?sequence=1&isAllowed=n
ER  -