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J. Biol. Chem., Vol. 278, Issue 15, 13133-13142, April 11, 2003
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From the We describe here the cloning and
characterization of a novel member of the thioredoxin family,
thioredoxin-like protein 2 (Txl-2). The Txl-2 open reading frame codes
for a protein of 330 amino acids consisting of two distinct domains: an
N-terminal domain typical of thioredoxins and a C-terminal domain
belonging to the nucleoside-diphosphate kinase family, separated
by a small interface domain. The Txl-2 gene spans ~28 kb, is
organized into 11 exons, and maps at locus 3q22.3-q23. A splicing
variant lacking exon 5 (
Characterization of Human Thioredoxin-like 2
A NOVEL MICROTUBULE-BINDING THIOREDOXIN EXPRESSED PREDOMINANTLY
IN THE CILIA OF LUNG AIRWAY EPITHELIUM AND SPERMATID MANCHETTE AND
AXONEME*,
,,,¶,,
,, and§§
Center for Biotechnology, the
§ Center for Structural Biology, Protein Analysis Unit,
Department of Biosciences at NOVUM, and the ¶ Department of
Medical Nutrition, Karolinska Institutet, Huddinge S-14157, Sweden, the
Department of Anatomy and Cell Biology, McGill University,
Montreal, Quebec H3A 2B2, Canada, the ** Department of
Anatomy and Cell Biology, Queen's University, Kingston, Ontario
K7L 3N6, Canada, and the Department of
Biochemistry and Molecular Biology, University of Calgary,
Calgary, Alberta T2N 4N1, Canada
5Txl-2) has also been isolated. By
quantitative real time PCR we demonstrate that Txl-2 mRNA is
ubiquitously expressed, with testis and lung having the highest levels
of expression. Unexpectedly, light and electron microscopy analyses
show that the protein is associated with microtubular structures such
as lung airway epithelium cilia and the manchette and axoneme of spermatids. Using in vitro translated proteins, we
demonstrate that full-length Txl-2 weakly associates with microtubules.
In contrast, 5Txl-2 specifically binds with very high affinity brain microtubule preparations containing microtubule-binding proteins. Importantly, 5Txl-2 also binds to pure microtubules, proving that it
possesses intrinsic microtubule binding capability. Taken together,
5Txl-2 is the first thioredoxin reported to bind microtubules and
might therefore be a novel regulator of microtubule physiology.
*
This work was supported by Swedish Medical Research Council
Grants 03P-14096-01A, 03X-14041-01A, and 13X-10370, the Åke Wibergs Stiftelse, and the Karolinska Institutet to (A. M.-V.), by
the Fundación Margit y Folke Pehrzon (to A. J.), and
by grants from the Canadian Institutes of Health Research (to
F. A. v. d. H. and R. O.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains Table 1.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF196568.
§§ To whom correspondence should be addressed: Center for Biotechnology, Dept. of Biosciences at NOVUM, Karolinska Institutet, Halsovagen 7, Huddinge S-14157, Sweden. Tel.: 46-8-608-3338; Fax: 46-8-774-5538; E-mail: anmi@biosci.ki.se.Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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