Journal
EMBO JOURNAL
Volume 20, Issue 15, Pages 4173-4182Publisher
WILEY
DOI: 10.1093/emboj/20.15.4173
Keywords
chromatin silencing; leukemia; oncogene; Pointed domain; polycomb group proteins
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Funding
- NCI NIH HHS [R01 CA081000, R01 CA81000] Funding Source: Medline
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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.
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