NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans

Shanshan Liu; Wen Zhang; Zengqiang Gao; Qianqian Ming; Haifeng Hou; Wenxian Lan; Houming Wu; Chunyang Cao; Yuhui Dong

doi:10.1016/j.febslet.2013.06.048

NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans

FEBS Lett. 2013 Aug 19;587(16):2635-42. doi: 10.1016/j.febslet.2013.06.048. Epub 2013 Jul 4.

Authors

Shanshan Liu¹, Wen Zhang, Zengqiang Gao, Qianqian Ming, Haifeng Hou, Wenxian Lan, Houming Wu, Chunyang Cao, Yuhui Dong

Affiliation

¹ State Key Laboratory of Bio-organic and Natural Product Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China.

PMID: 23831579
DOI: 10.1016/j.febslet.2013.06.048

Abstract

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 μM to all DNA substrates without any specificity. Biochemical assays suggested that HRDC1 cooperates with other domains to enhance full-length DrRecQ interactions with DNA.

Keywords: DNA; DrRecQ; HRDC1; NMR; Structure.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Bacterial Proteins / chemistry*
DNA / chemistry
Deinococcus / enzymology*
Models, Molecular
Molecular Sequence Data
Protein Structure, Secondary
RecQ Helicases / chemistry*
Sequence Homology, Amino Acid

Substances

Bacterial Proteins
DNA
RecQ Helicases