Skip Navigation


MBE Advance Access originally published online on April 27, 2005
Molecular Biology and Evolution 2005 22(7):1539-1542; doi:10.1093/molbev/msi151
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Supplementary Material
Right arrow An erratum has been published
Right arrow All Versions of this Article:
22/7/1539    most recent
msi151v1
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 (3)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Stover, N. A.
Right arrow Articles by Landweber, L. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stover, N. A.
Right arrow Articles by Landweber, L. F.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2005. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

Letter

Reciprocal Fusions of Two Genes in the Formaldehyde Detoxification Pathway in Ciliates and Diatoms

Nicholas A. Stover1, André R. O. Cavalcanti, Anya J. Li, Brian C. Richardson and Laura F. Landweber

Department of Ecology and Evolutionary Biology, Princeton University

E-mail: nick{at}genome.stanford.edu.

During the course of a pilot genome project for the ciliate Oxytricha trifallax, we discovered a fusion gene never before described in any taxa. This gene, FSF1, encodes a putative fusion protein comprising an entire formaldehyde dehydrogenase (FALDH) homolog at one end and an S-formylglutathione hydrolase (SFGH) homolog at the other, two proteins that catalyze serial steps in the formaldehyde detoxification pathway. We confirmed the presence of the Oxytricha fusion gene in vivo and detected transcripts of the full-length fusion gene. A survey of other large-scale sequencing projects revealed a similar fusion protein in a distantly related ciliate, Tetrahymena thermophila, and a possible fusion of these two genes in the diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana, but in the reverse order, with the SFGH domain encoded upstream of the FALDH domain. Orthologs of these fusion proteins may be widespread within the ciliates and diatoms.

Key Words: fusion gene • formaldehyde dehydrogenase • S-formylglutathione hydrolase • alcohol dehydrogenase III • esterase D • bikont phylogeny


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
J. Biol. Chem.Home page
C. F. Gonzalez, M. Proudfoot, G. Brown, Y. Korniyenko, H. Mori, A. V. Savchenko, and A. F. Yakunin
Molecular Basis of Formaldehyde Detoxification: CHARACTERIZATION OF TWO S-FORMYLGLUTATHIONE HYDROLASES FROM ESCHERICHIA COLI, FrmB AND YeiG
J. Biol. Chem., May 19, 2006; 281(20): 14514 - 14522.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
N. A. Stover, C. J. Krieger, G. Binkley, Q. Dong, D. G. Fisk, R. Nash, A. Sethuraman, S. Weng, and J. M. Cherry
Tetrahymena Genome Database (TGD): a new genomic resource for Tetrahymena thermophila research
Nucleic Acids Res., January 1, 2006; 34(suppl_1): D500 - D503.
[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.