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Journal of Cell Science, Vol 108, Issue 7 2683-2692, Copyright © 1995 by Company of Biologists

JOURNAL ARTICLES

Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein

J Marshall and DV Holberton
Department of Life Science, Nottingham University, U.K..

Previously described extended proteins from the cytoskeleton of Giardia lamblia (beta-giardin, median body protein) have been found to be segmented coiled coils with regular structural repeat patterns in their amino acid sequences. Screening a lambda ZAPII library derived from Giardia genomic DNA with an antibody directed against a 34 x 10(3) M(r) giardin isoform selected a gene encoding a much larger polypeptide chain (HPSR2), the sequence of which was determined by chromosome walking the open reading frame. The complete gene has been cloned and expressed as a recombinant protein of 183 x 10(3) M(r). The predicted amino acid sequence of the protein has identifiable features suggesting that it might be a motor protein with an amino-terminal hydrolytic domain attached to a long coiled coil stalk. The presumed head domain is 211 residues and contains a P-loop sequence conserved in purine nucleotide-binding proteins. The remaining 1409 amino acids mainly make up a region of heptad repeats such as in myosin or the kinesin stalk, ending in a small (67 amino acids) carboxy-terminal domain. Fourier analysis of the predicted stalk shows the presence of a strong physical repeat created by regular heptad phase changes dividing the coil into segments of 25 residues. This structure most closely resembles the smaller microtubule-associated median body protein which has segments of 24 residues.


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 Clin. Microbiol. Rev.Home page
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Clin. Microbiol. Rev., July 1, 2001; 14(3): 447 - 475.
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© The Company of Biologists Ltd 1995