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PfClpC Is an Essential Clp Chaperone Required for Plastid Integrity and Clp Protease Stability in Plasmodium falciparum.

Abstract：

:The deadly malaria parasite Plasmodium falciparum contains a nonphotosynthetic plastid, known as the apicoplast, that functions to produce essential metabolites, and drugs that target the apicoplast are clinically effective. Several prokaryotic caseinolytic protease (Clp) genes have been identified in the Plasmodium genome. Using phylogenetic analysis, we focused on the Clp members that may form a regulated proteolytic complex in the apicoplast. We genetically targeted members of this complex and generated conditional mutants of the apicoplast-localized PfClpC chaperone and PfClpP protease. Conditional inhibition of the PfClpC chaperone resulted in growth arrest and apicoplast loss and was rescued by addition of the essential apicoplast-derived metabolite IPP. Using a double-conditional mutant parasite line, we discovered that the chaperone activity is required to stabilize the mature protease, revealing functional interactions. These data demonstrate the essential function of PfClpC in maintaining apicoplast integrity and its role in regulating the proteolytic activity of the Clp complex.

journal_name

Cell Rep

journal_title

Cell reports

authors

Florentin A,Cobb DW,Fishburn JD,Cipriano MJ,Kim PS,Fierro MA,Striepen B,Muralidharan V

doi

10.1016/j.celrep.2017.10.081

subject

Has Abstract

pub_date

2017-11-14 00:00:00

pages

1746-1756

issue

7

issn

2211-1247

pii

S2211-1247(17)31544-9

journal_volume

21

pub_type

杂志文章

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