Structural highlights
Function
Q9RUU2_DEIRA
Publication Abstract from PubMed
The RecQ helicase from Deinococcus radiodurans (DrRecQ) distinguishes from other helicases in that it utilizes its three 'helicase and RNaseD C-terminal' domains (HRDC1, HRDC2 and HRDC3) to regulate its activity. These HRDC domains have different influence on the biochemical functions of DrRecQ. Currently, only the structure of HRDC3 was reported. Here, we determined the NMR structure of the N-terminal-most HRDC1, revealing a potential DNA binding domain. Fluorescence anisotropy assay indicates that HRDC1 has binding affinity weaker than 70 muM to all DNA substrates without any specificity. Biochemical assays suggested that HRDC1 cooperates with other domains to enhance full-length DrRecQ interactions with DNA.
NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.,Liu S, Zhang W, Gao Z, Ming Q, Hou H, Lan W, Wu H, Cao C, Dong Y FEBS Lett. 2013 Aug 19;587(16):2635-42. doi: 10.1016/j.febslet.2013.06.048. Epub , 2013 Jul 4. PMID:23831579[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu S, Zhang W, Gao Z, Ming Q, Hou H, Lan W, Wu H, Cao C, Dong Y. NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans. FEBS Lett. 2013 Aug 19;587(16):2635-42. PMID:23831579 doi:10.1016/j.febslet.2013.06.048
