کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5371721 | 1503965 | 2009 | 10 صفحه PDF | دانلود رایگان |
P. falciparum contains six copies of the Hsp70 gene of which PfHsp70-1 is important in the parasite's lifecycle. The protein consists of two domains like other Hsp70s but has an unusually long C-terminal tail. The full-length protein is stable towards high temperatures and chemical denaturants. Fluorescence and circular dichroism studies demonstrate that the â¼Â 42 kDa N-terminal/nucleotide-binding domain (NBD) is relatively unstable in isolation. Addition of the â¼Â 35 kDa C-terminal domain with an extended tail containing an EEVD motif confers thermal stability and makes it less susceptible to thermal denaturation. This suggests that the C-terminal domain functions as a stabilization domain. PfHsp70-1 possesses a chaperone activity in addition to other functions reported earlier. We report that the chaperone activity of PfHsp70-1 is enhanced in the presence of P. falciparum Hsp40 (Pfj1, PFD0465w), the homolog of bacterial DnaJ. The present work represents the first evidence for functional interactions between the PfHsp70-1 and Pfj1.
Journal: Biophysical Chemistry - Volume 142, Issues 1â3, June 2009, Pages 55-64