SPRTN is a mammalian DNA-binding metalloprotease that resolves DNA-protein crosslinks
elifesciences.org
SPRTN (also known as Dvc1 or C1orf124) was initially discovered as being an important protein for translesion DNA synthesis Based on the presence of an SprT-like metalloprotease domain with similarity to the WLM domain in Wss1, it was proposed that SPRTN and Wss1 could belong to a related family of
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- SPRTN (also known as Dvc1 or C1orf124) was initially discovered as being an important protein for translesion DNA synthesis
- Based on the presence of an SprT-like metalloprotease domain with similarity to the WLM domain in Wss1, it was proposed that SPRTN and Wss1 could belong to a related family of DPC-resolving proteases
- SPRTN preferentially binds to ubiquitin via its UBZ domain
- erall amino acid sequence conservation between SPRTN and Wss1 is relatively poor, particularly within the protease domains (Figure 1B), sharing only the conserved signature HEXXH motif found in the SprT family of metalloproteases, with glutamic acid being the catalytic amino acid.
- Taken together, we conclude that SPRTN cannot functionally complement Wss1 function due to either additional regulation of SPRTN not present in yeast or to inherently different pathways between yeast and metazoan cells involved in DPC resolution.
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