spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Crossley, R.
Right arrow Articles by Holberton, D. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Crossley, R.
Right arrow Articles by Holberton, D. V.

Journal of Cell Science, Vol 59, Issue 1 81-103, Copyright © 1983 by Company of Biologists

JOURNAL ARTICLES

Characterization of proteins from the cytoskeleton of Giardia lamblia

R Crossley and DV Holberton

Proteins from the axonemes and disc cytoskeleton of Giardia lamblia have been examined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. In addition to tubulin and the 30 X 10(3) molecular weight disc protein, at least 18 minor components copurify with the two major proteins in Triton-insoluble structures. The most prominent minor bands have the apparent molecular weights of 110 X 10(3), 95 X 10(3) and 81 X 10(3). Protein of 30 X 10(3) molecular weight accounts for about 20% of organelle protein on gels. In continuous 25 mM-Tris-glycine buffer it migrates mostly as a close-spaced doublet of polypeptides, which are here given the name giardins. Giardia tubulin and giardin have been purified by gel filtration chromatography in the presence of sodium dodecyl sulphate. Well-separated fractions were obtained that could be further characterized. Both proteins are heterogeneous when examined by isoelectric focusing. Five tubulin chains were detected by PAGE Blue 83 dye-binding after focusing in a broad-range ampholyte gel. Giardin is slightly less acidic than tubulin. On gels it splits into four major and four minor chains with isoelectric points in the pI range from 5.8 to 6.2. The amino acid composition of the giardin fraction has been determined, and compared to Giardia tubulin and a rat brain tubulin standard. Giardins are rich in helix-forming residues, particularly leucine. They have a low content of proline and glycine; therefore they may have extensive alpha-helical regions and be rod-shaped. As integral proteins of disc microribbons, giardins in vivo associate closely with tubulin. The properties of giardins indicate that in a number of respects - molecular size, charge, stoichiometry - their structural interaction with tubulin assemblies will be different from other tubulin-accessory protein copolymers studied in vitro.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
V. Seshadri, A. G. McArthur, M. L. Sogin, and R. D. Adam
Giardia lamblia RNA Polymerase II: AMANITIN-RESISTANT TRANSCRIPTION
J. Biol. Chem., July 18, 2003; 278(30): 27804 - 27810.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Mann, E. Gaskins, and C. Beckers
Proteolytic Processing of TgIMC1 during Maturation of the Membrane Skeleton of Toxoplasma gondii
J. Biol. Chem., October 18, 2002; 277(43): 41240 - 41246.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Microbiol. Rev.Home page
G. Faubert
Immune Response to Giardia duodenalis
Clin. Microbiol. Rev., January 1, 2000; 13(1): 35 - 54.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
J Marshall and D. Holberton
Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein
J. Cell Sci., January 7, 1995; 108(7): 2683 - 2692.
[Abstract] [PDF]


© The Company of Biologists Ltd 1983