Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (23)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by McArthur, A. G.
Right arrow Articles by Sogin, M. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McArthur, A. G.
Right arrow Articles by Sogin, M. L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Molecular Biology and Evolution 18:1455-1463 (2001)
© 2001 Society for Molecular Biology and Evolution

The Evolutionary Origins of Eukaryotic Protein Disulfide Isomerase Domains: New Evidence from the Amitochondriate Protist Giardia lamblia

Andrew G. McArthur, Leigh A. Knodler, Jeffrey D. Silberman, Barbara J. Davids, Frances D. Gillin and Mitchell L. Sogin

Josephine Bay Paul Center for Comparative Molecular Biology and Evolution, Marine Biological Laboratory, Woods Hole, Massachusetts
Department of Pathology, Division of Infectious Diseases and the Center for Molecular Genetics, University of California at San Diego
Institute of Geophysics and Planetary Physics and Department of Microbiology and Immunology, University of California at Los Angeles

A phylogenetic analysis of protein disulfide isomerase (PDI) domain evolution was performed with the inclusion of recently reported PDIs from the amitochondriate protist Giardia lamblia, yeast PDIs that contain a single thioredoxin-like domain, and PDIs from a diverse selection of protists. We additionally report and include two new giardial PDIs, each with a single thioredoxin-like domain. Inclusion of protist PDIs in our analyses revealed that the evolutionary history of the endoplasmic reticulum may not be simple. Phylogenetic analyses support common ancestry of all eukaryotic PDIs from a thioredoxin ancestor and independent duplications of thioredoxin-like domains within PDIs throughout eukaryote evolution. This was particularly evident for Acanthamoeba PDI, Dictyostelium PDI, and mammalian erp5 domains. In contrast, gene duplication, instead of domain duplication, produces PDI diversity in G. lamblia. Based on our results and the known diversity of PDIs, we present a new hypothesis that the five single-domain PDIs of G. lamblia may reflect an ancestral mechanism of protein folding in the eukaryotic endoplasmic reticulum. The PDI complement of G. lamblia and yeast suggests that a combination of PDIs may be used as a redox chain analogous to that known for bacterial Dsb proteins.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 ScienceHome page
H. G. Morrison, A. G. McArthur, F. D. Gillin, S. B. Aley, R. D. Adam, G. J. Olsen, A. A. Best, W. Z. Cande, F. Chen, M. J. Cipriano, et al.
Genomic Minimalism in the Early Diverging Intestinal Parasite Giardia lamblia
Science, September 28, 2007; 317(5846): 1921 - 1926.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Gottig, E. V. Elias, R. Quiroga, M. J. Nores, A. J. Solari, M. C. Touz, and H. D. Lujan
Active and Passive Mechanisms Drive Secretory Granule Biogenesis during Differentiation of the Intestinal Parasite Giardia lamblia
J. Biol. Chem., June 30, 2006; 281(26): 18156 - 18166.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Rubotham, K. Woods, J. A. Garcia-Salcedo, E. Pays, and D. P. Nolan
Characterization of Two Protein Disulfide Isomerases from the Endocytic Pathway of Bloodstream Forms of Trypanosoma brucei
J. Biol. Chem., March 18, 2005; 280(11): 10410 - 10418.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
N. L. Houston, C. Fan, Q.-Y. Xiang, J.-M. Schulze, R. Jung, and R. S. Boston
Phylogenetic Analyses Identify 10 Classes of the Protein Disulfide Isomerase Family in Plants, Including Single-Domain Protein Disulfide Isomerase-Related Proteins
Plant Physiology, February 1, 2005; 137(2): 762 - 778.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Padilla, R. Noiva, N. Lee, K. V. K. Mohan, H. L. Nakhasi, and A. Debrabant
An Atypical Protein Disulfide Isomerase from the Protozoan Parasite Leishmania Containing a Single Thioredoxin-like Domain
J. Biol. Chem., January 10, 2003; 278(3): 1872 - 1878.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. C. Touz, N. Gottig, T. E. Nash, and H. D. Lujan
Identification and Characterization of a Novel Secretory Granule Calcium-binding Protein from the Early Branching Eukaryote Giardia lamblia
J. Biol. Chem., December 20, 2002; 277(52): 50557 - 50563.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.