| Literature DB >> 11483520 |
C A Kim1, M L Phillips, W Kim, M Gingery, H H Tran, M A Robinson, S Faham, J U Bowie.
Abstract
TEL is a transcriptional repressor that is a frequent target of chromosomal translocations in a large number of hematalogical malignancies. These rearrangements fuse a potent oligomerization module, the SAM domain of TEL, to a variety of tyrosine kinases or transcriptional regulatory proteins. The self-associating property of TEL-SAM is essential for cell transformation in many, if not all of these diseases. Here we show that the TEL-SAM domain forms a helical, head-to-tail polymeric structure held together by strong intermolecular contacts, providing the first clear demonstration that SAM domains can polymerize. Our results also suggest a mechanism by which SAM domains could mediate the spreading of transcriptional repression complexes along the chromosome.Entities:
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Year: 2001 PMID: 11483520 PMCID: PMC149168 DOI: 10.1093/emboj/20.15.4173
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598