Abstract：
:ETV6 (or TEL), a transcriptional repressor belonging to the ETS family, is frequently involved in chromosomal translocations linked with human cancers. It displays a DNA-binding mode distinct from other ETS proteins due to the presence of a self-associating PNT domain. In this study, we used NMR spectroscopy to dissect the structural and dynamic bases for the autoinhibition of ETV6 DNA binding by sequences C-terminal to its ETS domain. The C-terminal inhibitory domain (CID) contains two helices, H4 and H5, which sterically block the DNA-binding interface of the ETS domain. Importantly, these appended helices are only marginally stable as revealed by amide hydrogen exchange and (15)N relaxation measurements. The CID is thus poised to undergo a facile conformational change as required for DNA binding. The CID also dampens millisecond timescale motions of the ETS domain hypothesized to be critical for the recognition of specific ETS target sequences. This work illustrates the use of appended sequences on conserved structural domains to generate biological diversity and complements previous studies of the allosteric mechanism of ETS1 autoinhibition to reveal both common and divergent features underlying the regulation of DNA binding by ETS transcription factors.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Coyne HJ 3rd,De S,Okon M,Green SM,Bhachech N,Graves BJ,McIntosh LPdoi
10.1016/j.jmb.2012.05.010subject
Has Abstractpub_date
2012-08-03 00:00:00pages
67-84issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(12)00395-6journal_volume
421pub_type
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