BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//CERN//INDICO//EN
BEGIN:VEVENT
SUMMARY:Linker switch mutations between canonical Plasmodium falciparum Hs
 p70-1 and PfHsp70-z reveal the role of this motif in regulating the functi
 onal specialisation of the two chaperones
DTSTART;VALUE=DATE-TIME:20260326T104000Z
DTEND;VALUE=DATE-TIME:20260326T110000Z
DTSTAMP;VALUE=DATE-TIME:20260425T232448Z
UID:indico-contribution-10336@events.saip.org.za
DESCRIPTION:Speakers: Addmore Shonhai (University of Venda)\nOf the five m
 alaria-causing species\, Plasmodium falciparum accounts for most malaria-r
 elated deaths. Central to the survival and infectivity of the parasite is 
 rapid replication coupled to upregulated protein production. Thus\, the de
 velopment of this malaria parasite is supported by the role of several hea
 t shock proteins (Hsps)\, which facilitate protein folding. P. falciparum 
 Hsp70-1 (PfHsp70-1) and PfHsp70-z are essential molecular chaperones (mole
 cules that assist proteins to fold correctly) that are cytosol-localized. 
 PfHsp70-z belongs to the Hsp110 cluster of Hsp70-like proteins.  Whereas P
 fHsp70-1 serves as a refolding chaperone\, PfHsp70-z is restricted to prev
 enting aggregation of proteins in the cell. The structural features underp
 inning the functional specialization of these chaperones remain elusive. P
 fHsp70-z possesses a unique linker segment. In the current study\, we expl
 ored the role of the linker in regulating the functional specialization of
  the two P. falciparum Hsp70s. Using recombinant forms of PfHsp70-1\, PfHs
 p70-z\, and E. coli Hsp70 (DnaK) as well as their linker switch mutant for
 ms\, we explored the effects of the linker mutations using circular dichro
 ism\, intrinsic and extrinsic fluorescence coupled to biochemical and in c
 ellulo analyses. Our findings demonstrate that the linker of PfHsp70-z mod
 ulates global conformation of the chaperone\, regulating several functions
  such as client protein binding\, chaperone\, and ATPase activities. In ad
 dition\, as opposed to the flexible linker of PfHsp70-1\, the PfHsp70-z li
 nker is rigid\, conferring notable conformational stability to this chaper
 one\, making it an effective holdase chaperone. Our findings highlight the
  role of the linker in regulating the functional specificity of Hsp70. We 
 discuss the implications of our findings to the development of the malaria
  parasite at the blood stages of the parasite.\n\nhttps://events.saip.org.
 za/event/272/contributions/10336/
LOCATION:
URL:https://events.saip.org.za/event/272/contributions/10336/
END:VEVENT
END:VCALENDAR