Open AccessP lasmodium falciparum single‐stranded DNA ‐binding protein ( PfSSB ) interacts with P f P rex helicase and modulates its activity
Author(s) -
Bhowmick Krishanu,
Dhar Suman K.
Publication year - 2014
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12343
Subject(s) - apicoplast , helicase , biology , plasmodium falciparum , microbiology and biotechnology , dna replication , organelle , dna binding protein , dna , rna helicase a , genetics , transcription factor , gene , plastid , rna , chloroplast , malaria , immunology
P lasmodium falciparum ( P f) apicoplast is an essential organelle harbouring a ~35‐kb circular genome. Prokaryotic nature of this organelle and its components makes it an attractive therapeutic target. The single‐stranded DNA ‐binding protein ( SSB ) and multidomain protein P f P rex are important apicoplast replication proteins. However, regulation of these proteins through protein–protein interaction remains largely unknown. Here, we report that P . falciparum single‐stranded DNA ‐binding protein ( PfSSB ) interacts with P f P rex helicase and modulates its activity. N‐terminal domain of PfSSB is involved in this interaction, whereas C‐terminal domain plays a pivotal role in the modulation of helicase activity. These results further, to our knowledge, understand apicoplast DNA replication.