2024-03-29T09:03:56Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/473182021-12-28T16:50:53Zcom_10261_11773com_10261_1col_10261_11774
DIGITAL.CSIC
author
Sadek, Christine M.
author
Jiménez, Alberto
author
Damdimopoulos, Anastasios E.
author
Kieselbach, Thomas
author
Nord, Magnus
author
Gustafsson, Jan-Åke
author
Spyrou, Giannis
author
Davis, Elaine C.
author
Oko, Richard
author
Hoorn, Frans A. van der
author
Miranda-Vizuete, Antonio
2012-03-22T08:53:00Z
2012-03-22T08:53:00Z
2003-02-04
Journal of Biological Chemistry 278(15): 13133-13142 (2003)
0021-9258
PMID: 12569107PMC3158135
http://hdl.handle.net/10261/47318
10.1074/jbc.M300369200
1083-351X
12569107
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 approximately 28 kb, is organized into 11 exons, and maps at locus 3q22.3-q23. A splicing variant lacking exon 5 (Delta 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, Delta 5Txl-2 specifically binds with very high affinity brain microtubule preparations containing microtubule-binding proteins. Importantly, Delta 5Txl-2 also binds to pure microtubules, proving that it possesses intrinsic microtubule binding capability. Taken together, Delta 5Txl-2 is the first thioredoxin reported to bind microtubules and might therefore be a novel regulator of microtubule physiology.
eng
openAccess
Thioredoxin
NDP kinase
Cilia
Flagella
Spermatozoa
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
artículo
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URL
https://digital.csic.es/bitstream/10261/47318/1/32.pdf
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https://digital.csic.es/bitstream/10261/47318/4/32.pdf.txt
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32.pdf.txt