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- 저자 : HaJeung Park (검색결과 4 건)
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이창우,Sun-Ha Park,Chang Sook Jeong,이창섭,Jong Wook Hong,Hyun Ho Park,박현,HaJeung Park,이준혁 한국구조생물학회 2018 Biodesign Vol.6 No.4
Spo0F is a response regulator that modulates sporulation, undergoes phosphorylation for phosphorelay signal transduction,and interacts with various regulatory proteins; however, the mechanisms through which phosphorylation induces structuralchanges and regulates interactions with binding partners remain unclear. Here, we determined the unphosphorylatedcrystal structure of Spo0F from the psychrophilic bacterium Paenisporosarcina sp. TG-14 (PaSpo0F) and establisheda phosphorylation-state structural model. We found that PaSpo0F underwent structural changes (Lys54 and Lys102)by phosphorylation and generated new interactions (Lys102/Gln10 and Lys54/Glu84) to stabilize the β4/α4 and β1/α1loop structures, which are important target-protein binding sites. Analysis of Bacillus subtilis Spo0 variants revealedmovement by BsSpo0F Thr82 and Tyr84 residues following interaction with BsSpo0B, providing insight into the movementof corresponding residues in PaSpo0F (Thr80 and Tyr82), with further analysis of BsSpo0F/BsRapH interaction revealingalterations in the β4/α4 loop region. These results suggest that phosphorylation-induced structural rearrangement mightbe essential for PaSpo0F activation and expand the understanding of Spo0F-specific activation mechanisms duringsporulation.
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Chang Woo Lee,Sun-Ha Park,Chang Sook Jeong,Chang Sup Lee,Jong Wook Hong,Hyun Ho Park,Hyun Park,HaJeung Park,Jun Hyuck Lee 한국구조생물학회 2018 Biodesign Vol.6 No.4
Spo0F is a response regulator that modulates sporulation, undergoes phosphorylation for phosphorelay signal transduction, and interacts with various regulatory proteins; however, the mechanisms through which phosphorylation induces structural changes and regulates interactions with binding partners remain unclear. Here, we determined the unphosphorylated crystal structure of Spo0F from the psychrophilic bacterium Paenisporosarcina sp. TG-14 (PaSpo0F) and established a phosphorylation-state structural model. We found that PaSpo0F underwent structural changes (Lys54 and Lys102) by phosphorylation and generated new interactions (Lys102/Gln10 and Lys54/Glu84) to stabilize the β4/α4 and β1/α1 loop structures, which are important target-protein binding sites. Analysis of Bacillus subtilis Spo0 variants revealed movement by BsSpo0F Thr82 and Tyr84 residues following interaction with BsSpo0B, providing insight into the movement of corresponding residues in PaSpo0F (Thr80 and Tyr82), with further analysis of BsSpo0F/BsRapH interaction revealing alterations in the β4/α4 loop region. These results suggest that phosphorylation-induced structural rearrangement might be essential for PaSpo0F activation and expand the understanding of Spo0F-specific activation mechanisms during sporulation.
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Molecular Mechanisms of Host Cytoskeletal Rearrangements by <i>Shigella</i> Invasins
Lee, Jun Hyuck,Park, HaJeung,Park, Yong Ho MDPI 2014 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.15 No.10
<P>Pathogen-induced reorganization of the host cell cytoskeleton is a common strategy utilized in host cell invasion by many facultative intracellular bacteria, such as <I>Shigella</I>, <I>Listeria</I>, enteroinvasive <I>E. coli</I> and <I>Salmonella</I>. <I>Shigella</I> is an enteroinvasive intracellular pathogen that preferentially infects human epithelial cells and causes bacillary dysentery. Invasion of <I>Shigella</I> into intestinal epithelial cells requires extensive remodeling of the actin cytoskeleton with the aid of pathogenic effector proteins injected into the host cell by the activity of the type III secretion system. These so-called <I>Shigella</I> invasins, including IpaA, IpaC, IpgB1, IpgB2 and IpgD, modulate the actin-regulatory system in a concerted manner to guarantee efficient entry of the bacteria into host cells.</P>
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Structural insights into the psychrophilic germinal protease PaGPR and its autoinhibitory loop
Chang Woo Lee,Saeyoung Lee,Chang-Sook Jeong,Jisub Hwang,Jeong Ho Chang,In-Geol Choi,T. Doohun Kim,HaJeung Park,Hye-Yeon Kim,Jun Hyuck Lee 한국미생물학회 2020 The journal of microbiology Vol.58 No.9
In spore forming microbes, germination protease (GPR) plays a key role in the initiation of the germination process. A critical step during germination is the degradation of small acidsoluble proteins (SASPs), which protect spore DNA from external stresses (UV, heat, low temperature, etc.). Inactive zymogen GPR can be activated by autoprocessing of the N-terminal pro-sequence domain. Activated GPR initiates the degradation of SASPs; however, the detailed mechanisms underlying the activation, catalysis, regulation, and substrate recognition of GPR remain elusive. In this study, we determined the crystal structure of GPR from Paenisporosarcina sp. TG-20 (PaGPR) in its inactive form at a resolution of 2.5 Å. Structural analysis showed that the active site of PaGPR is sterically occluded by an inhibitory loop region (residues 202–216). The N-terminal region interacts directly with the self-inhibitory loop region, suggesting that the removal of the N-terminal pro-sequence induces conformational changes, which lead to the release of the self-inhibitory loop region from the active site. In addition, comparative sequence and structural analyses revealed that PaGPR contains two highly conserved Asp residues (D123 and D182) in the active site, similar to the putative aspartic acid protease GPR from Bacillus megaterium. The catalytic domain structure of PaGPR also shares similarities with the sequentially non-homologous proteins HycI and HybD. HycI and HybD are metalloproteases that also contain two Asp (or Glu) residues in their active site, playing a role in metal binding. In summary, our results provide useful insights into the activation process of PaGPR and its active conformation.
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