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KMID : 0880220170550060464
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Journal of Microbiology
2017 Volume.55 No. 6 p.464 ~ p.474
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Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier
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Lee Chang-Woo
Park Sun-Ha
Lee Sung-Gu
Shin Seung-Chul
Han Se-Jong
Kim Han-Woo
Park Hyun-Ho
Kim Sung-Hwan
Kim Hak-Jun
Park Hyun
Park Ha-Jeung
Lee Jun-Hyuck
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Abstract
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The two-component phosphorelay system is the most prevalent mechanism for sensing and transducing environmental signals in bacteria. Spore formation, which relies on the two-component phosphorelay system, enables the long-term survival of the glacial bacterium Paenisporosarcina sp. TG-14 in the extreme cold environment. Spo0A is a key response regulator of the phosphorelay system in the early stage of spore formation. The protein is composed of a regulatory N-terminal phospho-receiver domain and a DNA-binding C-terminal activator domain. We solved the three-dimensional structure of the unphosphorylated (inactive) form of the receiver domain of Spo0A (PaSpo0A-R) from Paenisporosarcina sp. TG-14. A structural comparison with phosphorylated (active form) Spo0A from Bacillus stearothermophilus (BsSpo0A) showed minor notable differences. A molecular dynamics study of a model of the active form and the crystal structures revealed significant differences in the α4 helix and the preceding loop region where phosphorylation occurs. Although an oligomerization study of PaSpo0A-R by analytical ultracentrifugation (AUC) has shown that the protein is in a monomeric state in solution, both crosslinking and crystal-packing analyses indicate the possibility of weak dimer formation by a previously undocumented mechanism. Collectively, these observations provide insight into the mechanism of phosphorylation-dependent activation unique to Spo0A.
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KEYWORD
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analytical ultracentrifugation, Paenisporosarcina sp. TG-14, spore formation, Spo0A, X-ray crystallography
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