Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein familyopen access
- Authors
- Park, Nohra; Heo, Jihune; Song, Saemee; Jo, Inseong; Lee, Kangseok; Ha, Nam-Chul
- Issue Date
- May-2017
- Publisher
- MICROBIOLOGICAL SOCIETY KOREA
- Keywords
- Rnase ES inhibitor; crystal structure; Streptomyces coelicolor
- Citation
- JOURNAL OF MICROBIOLOGY, v.55, no.5, pp 388 - 395
- Pages
- 8
- Journal Title
- JOURNAL OF MICROBIOLOGY
- Volume
- 55
- Number
- 5
- Start Page
- 388
- End Page
- 395
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/4497
- DOI
- 10.1007/s12275-017-7053-8
- ISSN
- 1225-8873
1976-3794
- Abstract
- Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-terminal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, exhibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long alpha-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Truncation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our findings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension alpha-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor.
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