Kaushik, Sandeep and Krishnarjuna, Bankala and Raghothama, Srinivasarao and Aggarwal, Sangita and Raghunathan, Vidya and Ganjiwale, Anjali (2012) Theoretical and in vitro studies of a C-terminal peptide from PGKC of Leishmania mexicana mexicana. In: MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 185 (1). pp. 27-35.
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Trypanosomatids cause deadly diseases in humans. Of the various biochemical pathways in trypanosomatids, glycolysis, has received special attention because of being sequestered in peroxisome like organelles critical for the survival of the parasites. This study focuses on phosphoglycerate kinase (PGK) from Leishmania spp. which, exists in two isoforms, the cytoplasmic PGKB and glycosomal PGKC differing in their biochemical properties. Computational analysis predicted the likelihood of a transmembrane helix only in the glycosomal isoform PGKC, of approximate length 20 residues in the 62-residue extension, ending at, arginine residues R471 and R472. From experimental studies using circular dichroism and NMR with deuterated sodium dodecyl sulfate, we find that the transmembrane helix spans residues 448 +/- 2 to 476 in Leishmania mexicana PGKC. The significance of this observation is discussed in the context of glycosomal transport and substrate tunneling. (C) 2012 Elsevier B.V. All rights reserved.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to Elsevier SCience|
|Keywords:||Phosphoglycerate kinase; C-terminal domain; Transmembrane helix; Glycosomal localization; NMR structure|
|Department/Centre:||Division of Chemical Sciences > NMR Research Centre (Formerly SIF)|
|Date Deposited:||11 Sep 2012 07:55|
|Last Modified:||11 Sep 2012 07:55|
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