Isolation and characterization of the mouse translin-associated protein X (Trax) gene

Isolation and characterization of the mouse translin-associated protein X (Trax) gene Mammalian Genome 11, 395–398 (2000). Incorporating Mouse Genome © Springer-Verlag New York Inc. 2000 Isolation and characterization of the mouse translin-associated protein X(Trax) gene Rebecca S. Devon,* Martin S. Taylor, J. Kirsty Millar, David J. Porteous MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK Received: 15 October 1999 / Accepted: 20 December 1999 The translin-associated protein X (Trax) has been identified as a factor of unknown function that forms complexes with the protein translin (Aoki et al. 1997; Taira et al. 1998). Translin itself was originally identified as a protein that binds specifically to consen- sus sequences found at the breakpoints of many chromosomal translocations, potentially playing a role in the recognition of stag- gered DNA ends (Aoki et al. 1995). In addition, translin is trans- ported to the nucleus after DNA damage and may thus function in DNA repair (Kasai et al. 1997). In addition to binding DNA, translin is also capable of binding to highly conserved sequences in the 38 untranslated regions (UTRs) of certain RNAs, thereby suppressing their in vitro trans- lation. The mouse homolog of translin (also called testis-brain RNA binding protein, TB-RBP; Wu et al. 1997), together with an http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Mammalian Genome Springer Journals

Isolation and characterization of the mouse translin-associated protein X (Trax) gene

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Publisher
Springer Journals
Copyright
Copyright © 2000 by Springer-Verlag New York Inc.
Subject
Life Sciences; Cell Biology; Animal Genetics and Genomics; Human Genetics
ISSN
0938-8990
eISSN
1432-1777
D.O.I.
10.1007/s003350010074
Publisher site
See Article on Publisher Site

Abstract

Mammalian Genome 11, 395–398 (2000). Incorporating Mouse Genome © Springer-Verlag New York Inc. 2000 Isolation and characterization of the mouse translin-associated protein X(Trax) gene Rebecca S. Devon,* Martin S. Taylor, J. Kirsty Millar, David J. Porteous MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK Received: 15 October 1999 / Accepted: 20 December 1999 The translin-associated protein X (Trax) has been identified as a factor of unknown function that forms complexes with the protein translin (Aoki et al. 1997; Taira et al. 1998). Translin itself was originally identified as a protein that binds specifically to consen- sus sequences found at the breakpoints of many chromosomal translocations, potentially playing a role in the recognition of stag- gered DNA ends (Aoki et al. 1995). In addition, translin is trans- ported to the nucleus after DNA damage and may thus function in DNA repair (Kasai et al. 1997). In addition to binding DNA, translin is also capable of binding to highly conserved sequences in the 38 untranslated regions (UTRs) of certain RNAs, thereby suppressing their in vitro trans- lation. The mouse homolog of translin (also called testis-brain RNA binding protein, TB-RBP; Wu et al. 1997), together with an

Journal

Mammalian GenomeSpringer Journals

Published: May 1, 2000

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