NDLI: An unconventional form of actin in protozoan hemoflagellate, Leishmania.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gupta, Chhitar M. Mitra, Kalyan Kumar, Ashutosh Kapoor, Prabodh Siddiqi, Mohammad Imran Sahasrabuddhe, Amogh A.
Description	Author Affiliation: Kapoor P ( Division of Molecular and Structural Biology, Central Drug Research Institute, Lucknow-226001, India.)
Abstract	Leishmania actin was cloned, overexpressed in baculovirus-insect cell system, and purified to homogeneity. The purified protein polymerized optimally in the presence of Mg2+ and ATP, but differed from conventional actins in its following properties: (i) it did not polymerize in the presence of Mg2+ alone, (ii) it polymerized in a restricted range of pH 7.0-8.5, (iii) its critical concentration for polymerization was found to be 3-4-fold lower than of muscle actin, (iv) it predominantly formed bundles rather than single filaments at pH 8.0, (v) it displayed considerably higher ATPase activity during polymerization, (vi) it did not inhibit DNase-I activity, and (vii) it did not bind the F-actin-binding toxin phalloidin or the actin polymerization disrupting agent Latrunculin B. Computational and molecular modeling studies revealed that the observed unconventional behavior of Leishmania actin is related to the diverged amino acid stretches in its sequence, which may lead to changes in the overall charge distribution on its solvent-exposed surface, ATP binding cleft, Mg2+ binding sites, and the hydrophobic loop that is involved in monomer-monomer interactions. Phylogenetically, it is related to ciliate actins, but to the best of our knowledge, no other actin with such unconventional properties has been reported to date. It is therefore suggested that actin in Leishmania may serve as a novel target for design of new antileishmanial drugs.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	33
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-08-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Actins Chemistry Metabolism Leishmania Donovani Protozoan Proteins Ultrastructure Adenosine Triphosphate Animals Computer Simulation Hydrogen-Ion Concentration Kinetics Physiology Magnesium Molecular Sequence Data Polymerase Chain Reaction Spodoptera Parasitology Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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