Adams & Adams biotechnology specialist contributes to a scientific research paper
10/06/2009

Dr William Modisakeng, a biotechnology specialist at Adams & Adams, together with a group of scientists from Rhodes University (RSA) in South Africa, Beneroya Research Institute (USA) and the Rochester University Medical Center (USA) have recently published a peer reviewed research paper in the Journal of Molecular Genetics and Genomics.

In the publication the authors presented data that demonstrates for the first time that the coelacanth encodes a functional molecular chaperone system.
ABSTRACT:
Isolation of a Latimeria menadoensis heat shock protein 70 (Lmhsp70) that has all the features of an inducible gene and encodes a functional molecular chaperone
Keoagile W. Modisakeng, Meesbah Jiwaji, Eva-Rachele Pesce, Jacques Robert, Chris T. Amemiya, Rosemary A. Dorrington and Gregory L. Blatch

Molecular chaperones facilitate the correct folding of other proteins, and heat shock proteins form one of the major classes of molecular chaperones. Heat shock protein 70 (Hsp70) has been extensively studied, and shown to be critically important for cellular protein homeostasis in almost all prokaryotic and eukaryotic systems studied to date. Since there have been very limited studies conducted on coelacanth chaperones, the main objective of this study was to genetically and biochemically characterize a coelacanth Hsp70. We have successfully isolated an Indonesian coelacanth (L. menadoensis) hsp70 , gene Lmhsp70, and found that it contained an intronless coding region and a potential upstream regulatory region. Lmhsp70 encoded a typical Hsp70 based on conserved structural and functional features, and the predicted upstream regulatory region was found to contain six potential promoter elements, and three potential heat shock elements (HSEs). The intronless nature of the coding region and the presence of HSEs suggested that Lmhsp70 was stress-inducible. Phylogenetic analyses provided further evidence that Lmhsp70 was probably inducible, and that it branched as a clade intermediate between bony fish and tetrapods. Recombinant LmHsp70 was successfully overproduced, purified and found to be functional using ATPase activity assays. Taken together, these data provide evidence for the first time that the coelacanth encodes a functional molecular chaperone system.

Mol. Genet. Genomics, Accepted 26 April 2009