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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

  • Microbial Physiology and Biochemistry
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Abstract

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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Authors and Affiliations

  1. Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea

    Chang Woo Lee, Sun-Ha Park, Sung Gu Lee, Seung Chul Shin, Han-Woo Kim, Hyun Park & Jun Hyuck Lee

  2. Department of Polar Sciences, Korea University of Science and Technology, Incheon, 21990, Republic of Korea

    Chang Woo Lee, Sung Gu Lee, Se Jong Han, Han-Woo Kim, Hyun Park & Jun Hyuck Lee

  3. Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, Republic of Korea

    Se Jong Han

  4. Department of Biochemistry, School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, 38541, Republic of Korea

    Hyun Ho Park

  5. New Drug Development Center, Daegu-Gyungpook Medical Innovation Foundation, Daegu, 41061, Republic of Korea

    Sunghwan Kim

  6. Department of Chemistry, Pukyong National University, Busan, 608-739, Republic of Korea

    Hak Jun Kim

  7. X-Ray Core, TRI, The Scripps Research Institute, Jupiter, FL, 33458, USA

    HaJeung Park

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  1. Chang Woo Lee
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Lee, C.W., Park, SH., Lee, S.G. et al. 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. J Microbiol. 55, 464–474 (2017). https://doi.org/10.1007/s12275-017-6599-9

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