Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print May 14, 2004
Mol. Biol. Cell 10.1091/mbc.E04-03-0217

A more recent version of this article appeared on July 1, 2004
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E04-03-0217v1
15/7/3257    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Google Scholar
Google Scholar
Right arrow Articles by Pullen, T. J.
Right arrow Articles by Gull, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pullen, T. J.
Right arrow Articles by Gull, K.

Submitted on March 15, 2004
Revised on April 26, 2004
Accepted on April 26, 2004

Protein targeting of an unusual, evolutionarily conserved adenylate kinase to a eukaryotic flagellum

Timothy J. Pullen{dagger}, Michael L. Ginger{dagger}, Simon J. Gaskell{ddagger}, and Keith Gull{dagger}*

{dagger}Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.; {ddagger}Department of Chemistry, UMIST, P. O. Box 88, Sackville Street, Manchester, M60 1QD, UK

Monitoring Editor: Paul Matsudaira

The eukaryotic flagellum is a large structure into which specific constituent proteins must be targeted, transported and assembled after their synthesis in the cytoplasm. Using Trypanosoma brucei and a proteomic approach, we have identified and characterized a novel set of adenylate kinase proteins that are localized to the flagellum. These proteins represent unique isoforms that are targeted to the flagellum by an N-terminal extension to the protein and are incorporated into an extraaxonemal structure (the paraflagellar rod). We show that the N-terminal extension is both necessary for isoform location in the flagellum and sufficient for targeting of a GFP reporter protein to the flagellum. Moreover, these N-terminal extension sequences are conserved in evolution and we find that they allow the identification of novel adenylate kinases in the genomes of humans and worms. Given the existence of specific isoforms of certain central metabolic enzymes, and targeting sequences for these isoforms, we suggest that these isoforms form part of a complex, "solid-phase" metabolic capability that is built into the eukaryotic flagellum.

*Corresponding author. E-mail address: keith.gull{at}pathology.ox.ac.uk






Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.