title: 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.
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.
authors.affiliation: Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.|Department of Polar Sciences, Korea University of Science and Technology, Incheon, 21990, Republic of Korea.
authors.forename: Chang Woo
authors.initials: CW
authors.lastname: Lee
authors.affiliation: Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.
authors.forename: Sun-Ha
authors.initials: SH
authors.lastname: Park
authors.affiliation: Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.|Department of Polar Sciences, Korea University of Science and Technology, Incheon, 21990, Republic of Korea.
authors.forename: Sung Gu
authors.initials: SG
authors.lastname: Lee
authors.affiliation: Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.
authors.forename: Seung Chul
authors.initials: SC
authors.lastname: Shin
authors.affiliation: Department of Polar Sciences, Korea University of Science and Technology, Incheon, 21990, Republic of Korea.|Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.
authors.forename: Se Jong
authors.initials: SJ
authors.lastname: Han
authors.affiliation: Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.|Department of Polar Sciences, Korea University of Science and Technology, Incheon, 21990, Republic of Korea.
authors.forename: Han-Woo
authors.initials: HW
authors.lastname: Kim
authors.affiliation: Department of Biochemistry, School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, 38541, Republic of Korea.
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
authors.affiliation: New Drug Development Center, Daegu-Gyungpook Medical Innovation Foundation, Daegu, 41061, Republic of Korea.
authors.forename: Sunghwan
authors.initials: S
authors.lastname: Kim
authors.affiliation: Department of Chemistry, Pukyong National University, Busan, 608-739, Republic of Korea.
authors.forename: Hak Jun
authors.initials: HJ
authors.lastname: Kim
authors.affiliation: Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.|Department of Polar Sciences, Korea University of Science and Technology, Incheon, 21990, Republic of Korea.
authors.forename: Hyun
authors.initials: H
authors.lastname: Park
authors.affiliation: X-Ray Core, TRI, The Scripps Research Institute, Jupiter, FL, 33458, USA. hajpark@scripps.edu.
authors.forename: HaJeung
authors.initials: H
authors.lastname: Park
authors.affiliation: Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea. junhyucklee@kopri.re.kr.|Department of Polar Sciences, Korea University of Science and Technology, Incheon, 21990, Republic of Korea. junhyucklee@kopri.re.kr.
authors.forename: Jun Hyuck
authors.initials: JH
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D000864:Antarctic Regions; D001426:Bacterial Proteins / Q000235:genetics; D003080:Cold Temperature; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000235:genetics*; D046448:Ice Cover / Q000382:microbiology*; D056004:Molecular Dynamics Simulation; D010766:Phosphorylation; D058641:Planococcaceae / Q000235:genetics* / Q000302:isolation & purification; D000072417:Protein Domains / Q000235:genetics*; D017433:Protein Structure, Secondary; D015398:Signal Transduction / Q000235:genetics; D013171:Spores, Bacterial / Q000254:growth & development*; D014157:Transcription Factors / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D014157:Transcription Factors
keywords: Paenisporosarcina sp. TG-14; Spo0A; X-ray crystallography; analytical ultracentrifugation; spore formation