Abstract
DNA damage suppressor protein (Dsup) from water bear Ramazzottius varieormatus can suppress X-ray-induced DNA damage and improve radio-tolerance in human cells [Hashimoto, et al. Nat Commun 7, 12808 (2016)]. The functional information about this unique protein is very limited and its structure is unknown. Sequence analysis suggests that Dsup is an intrinsically disordered protein with extended unstructured regions and a potential single-helix domain. We are studying Dsup using a variety of biophysical methods to understand the basis of its interaction with DNA and the mechanism of DNA protection.
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