TY  - JOUR
AU  - Mullin, KA
AU  - Lim, L
AU  - Ralph, SA
AU  - Spurck, TP
AU  - Handman, E
AU  - McFadden, GI
Y2  - 2014/05/21
Y1  - 2006/06/20
SN  - 0027-8424
UR  - http://hdl.handle.net/11343/26502
AB  - Malaria parasites contain a nonphotosynthetic plastid homologous to chloroplasts of plants. The parasite plastid synthesizes fatty acids, heme, iron sulfur clusters and isoprenoid precursors and is indispensable, making it an attractive target for antiparasite drugs. How parasite plastid biosynthetic pathways are fuelled in the absence of photosynthetic capture of energy and carbon was not clear. Here, we describe a pair of parasite transporter proteins, PfiTPT and PfoTPT, that are homologues of plant chloroplast innermost membrane transporters responsible for moving phosphorylated C3, C5, and C6 compounds across the plant chloroplast envelope. PfiTPT is shown to be localized in the innermost membrane of the parasite plastid courtesy of a cleavable N-terminal targeting sequence. PfoTPT lacks such a targeting sequence, but is shown to localize in the outermost parasite plastid membrane with its termini projecting into the cytosol. We have identified these membrane proteins in the parasite plastid and determined membrane orientation for PfoTPT. PfiTPT and PfoTPT are proposed to act in tandem to transport phosphorylated C3 compounds from the parasite cytosol into the plastid. Thus, the transporters could shunt glycolytic derivatives of glucose scavenged from the host into the plastid providing carbon, reducing equivalents and ATP to power the organelle.
N1  - application/pdf
LA  - English
PB  - NATL ACAD SCIENCES
KW  - Protein Targeting and Signal Transduction; Infectious Diseases
T1  - Membrane transporters in the relict plastid of malaria parasites
DO  - 10.1073/pnas.0602293103
IS  - PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
VL  - 103
IS  - 25
SP  - 9572-9577
L1  - /bitstream/handle/11343/26502/116306_5349.pdf?sequence=1&isAllowed=n
ER  -