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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003785naa a2200421 4500
001oai:DiVA.org:liu-98799
003SwePub
008131014s2003 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:1960571
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-987992 URI
0247 a https://doi.org/10.1074/jbc.M3003692002 DOI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:19605712 URI
040 a (SwePub)liud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Sadek, Christine M.u Karolinska Institutet, Huddinge, Sweden4 aut
2451 0a 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
264 1b American Society for Biochemistry and Molecular Biology,c 2003
338 a print2 rdacarrier
520 a 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.
7001 a Jiménez, Albertou Karolinska Institutet4 aut
7001 a Damdimopoulos, Anastasios Eu Karolinska Institutet4 aut
7001 a Kieselbach, Thomasu Karolinska Institutet, Huddinge, Sweden4 aut
7001 a Nord, Magnusu Karolinska Institutet4 aut
7001 a Gustafsson, Jan-Åkeu Karolinska Institutet, Huddinge, Sweden4 aut
7001 a Spyrou, Giannisu Department of Biosciences at Novum, Center for Biotechnology, Karolinska Institutet, Huddinge, Sweden4 aut0 (Swepub:liu)ioasp42
7001 a Davis, Elaine C.u McGill University, Montreal, Quebec, Canada4 aut
7001 a Oko, Richardu Queen's University, Kingston, Ontario, Canada4 aut
7001 a van der Hoorn, Frans A.u University of Calgary, Alberta, Canada4 aut
7001 a Miranda-Vizuete, Antoniou Karolinska Institutet, Huddinge, Sweden4 aut
7001 a Spyrou, I4 aut
7102 a Karolinska Institutetb Karolinska Institutet, Huddinge, Sweden4 org
7730 t Journal of Biological Chemistryd : American Society for Biochemistry and Molecular Biologyg 278:15, s. 13133-13142q 278:15<13133-13142x 0021-9258x 1083-351X
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-98799
8564 8u https://doi.org/10.1074/jbc.M300369200
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:1960571

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