Nucleic Acids Research, 2002, Vol. 30, No. 4 993-1000
© 2002 Oxford University Press
Complex regulation of the human gene for the Z-DNA binding protein DLM-1
Institute for Immunology, University Hospital Hamburg-Eppendorf, Martinistrasse 52, D-20246 Hamburg, Germany and 1Laboratory of Cell Biology, The Rockefeller University, New York, NY 10021, USA
Dlm-1 is a recently described gene which is upregulated in murine stromal cells lining tumors. The function of the 40 kDa DLM-1 protein is poorly understood. DLM-1 contains an N-terminal Z-DNA binding domain homologous to the Z
domain in the RNA editing enzyme ADAR1. We report the cloning of human and rat DLM-1. In addition to the Z domain, three further conserved regions were identified. One of these is homologous to the second Z-DNA binding domain, Zß, of ADAR1. We find that human DLM-1 is predominantly expressed in lymphatic tissues. The gene spans 17 kb and consists of 10 exons. DNA transcripts are extremely heterogeneous as a result of alternative splicing and the usage of exon variants combined with at least two transcriptional start sites and 3'-terminal exons. The exon coding for the Z domain was present in approximately one-third of the analyzed mRNAs. Nearly half of the transcripts contained exon variants that had premature stop codons incorporated. Based on our analysis, over 2000 different mRNAs may be produced due to alternative splicing and usage of different 5' and 3' ends. The cellular function of DLM-1 appears to call for a high degree of adaptation by this complex regulation.
* To whom correspondence should be addressed. Tel: +49 40 42803 4595; Fax: +49 40 42803 4243; Email: haag{at}uke.uni-hamburg.de
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