• Title/Summary/Keyword: cyclic(Phe-Pro)

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H-NS Silences Gene Expression of LeuO, the Master Regulator of the Cyclic(Phe-Pro)-dependent Signal Pathway, in Vibrio vulnificus

  • Park, Na-Young;Lee, Keun-Woo;Kim, Kun-Soo
    • Journal of Microbiology and Biotechnology
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    • v.30 no.6
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    • pp.830-838
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    • 2020
  • The histone-like nucleoid structuring protein (H-NS) is an abundant global regulator of environmentally controlled gene expression. Herein, we demonstrate that H-NS represses the expression of LeuO, the master regulator of the cyclic(Phe-Pro)-dependent signaling pathway, by directly binding to the upstream region of the gene. H-NS binds to a long stretched region (more than 160-bp long), which overlaps with binding sites for ToxR and LeuO. A high quantity of H-NS outcompetes ToxR for binding to the cis-acting element of leuO. However, our footprinting analyses suggests that the binding of H-NS is relatively weaker than LeuO or ToxR at the same molarity. Considering that the DNA nucleotide sequences of the upstream regions of leuO genes are highly conserved among various Vibrio, such patterns as those found in V. vulnificus would be a common feature in the regulation of leuO gene expression in Vibrionaceae. Taken together, these results suggest that, in species belonging to Vibrionaceae, H-NS regulates the expression of leuO as a basal stopper when cFP-ToxR mediated signaling is absent.

Conformational Study of Cyclic Ac-Cys-Pro-Xaa-Cys-NHMe Peptides: a Model for Chain Reversal and Active Site of Disulfide Oxidoreductase

  • Park, Hae-Sook;Kim, Choon-mi;Kee, Kang-Young
    • Proceedings of the PSK Conference
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    • 2002.10a
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    • pp.330.2-330.2
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    • 2002
  • The conformational study on cyclic Ac-Cys-Pro-Xaa-Cys-NHMe (Ac-CPXC-NHMe: X = Ala, Val. Leu. Aib. Gly. His. Phe, Tyr. Asn. and Ser) peptides has been carried out using the ECEPP/3 force field and the hydration shell model in the unhydrated and hydrated states. This work has been undertaken to investigate structural implications of the CPXC sequence as the chain reversal for the initiation of protein folding and as the motif for active site of disulfide oxidoreductases. The backbone conformation DAAA is in common the most feasible for cyclic CPXC peptides in the hydrated state. which has a type 1${\beta}$-turn at the Pro-Xaa sequence. The proline residue and the hydrogen bond between backbones of two cystines appear to play a role in stabilizing this preferred conformation of cycilc CPXC peptides. However. the distributions of backbone conformations and ${\beta}$-turns may indicate that the cyclic CPXC peptide seems to exist as an ensemble of ${\beta}$-turns and coiled conformations. The intirnsic stability of the cyclic CPXC motif itself the active conformation appears to play a role in determining electrochemical properties of disulfide oxidoreductases.

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Preferred Conformations of Cyclic Ac-Cys-Pro-Xaa-Cys-NHMe Peptides: a Model for Chain Reversal and Active Site of Disulfide Oxidoreductase

  • Park, Hae-Sook;Kim, Choonmi;Kang, Young-Kee
    • Proceedings of the Korean Biophysical Society Conference
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    • 2001.06a
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    • pp.35-35
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    • 2001
  • The conformational study on cyclic Ac-Cys-Pro-Xaa-Cys-NHMe (Ac-CPXC-NHMe; X = Ala, Val, Leu, Aib, Gly, His, Phe, Tyr, Asn, and Ser) peptides has been carried out using the ECEPP/3 force field and the hydration shell model in the unhydrated and hydrated states. This work has been undertaken to investigate structural implications of the CPXC sequence as the chain reversal for the initiation of protein folding and as the motif for active site of disulfide oxidoreductases.(omitted)

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Bioactive Cyclic Dipeptides from a Marine Sponge-Associated Bacterium, Psychrobacter sp.

  • Li, Huayue;Lee, Byung-Cheol;Kim, Tae-Sung;Bae, Kyung-Sook;Hong, Jong-Ki;Choi, Sang-Ho;Bao, Baoquan;Jung, Jee-Hyung
    • Biomolecules & Therapeutics
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    • v.16 no.4
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    • pp.356-363
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    • 2008
  • A bacterial strain with good antibacterial activities against Staphylococus aureus and Escherichia coli was isolated from a marine sponge Stelleta sp., and it was identified as a Psychrobacter sp. by comparative 16S rDNA sequence analysis. In our search for bioactive secondary metabolites from this psychrophillic and halotolerent bacterium, sixteen cyclic dipeptides (1-16) were isolated and their structures were identified on the basis of NMR analysis. In the test of the compounds for the protective effect against Vibrio vulnificusinduced cytotoxicity in human intestinal epithelial cells, cyclo-(L-Pro-L-Phe) (5) exhibited significant protective effect. Compounds 2, 6, and 11, which contain D-amino acid, were first isolated from bacteria.

Selective Inhibition of Bicyclic Tetrapeptide Histone Deacetylase Inhibitor on HDAC4 and K562 Leukemia Cell

  • Li, Xiao-Hui;Huang, Mei-Ling;Wang, Shi-Miao;Wang, Qing
    • Asian Pacific Journal of Cancer Prevention
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    • v.14 no.12
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    • pp.7095-7100
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    • 2013
  • Histone deacetylase (HDAC) inhibitors of cyclic peptide have been proved to be the most complex but the most stable and relative efficient inhibitors because of their large cap region. In this paper, a series of studies were carried out to evaluate the efficacy of synthetic bicyclic tetrapeptide inhibitors 1-5 containing hydroxamic acid referring molecular docking, anti-proliferation, morphology and apoptosis. Docking analysis, together with enzyme inhibitory results, verified the selective capability of inhibitor 4 to HDAC4, which might closely related to haematological tumorigenesis, with Phe227, Asp115, Pro32, His198 and Ser114 participating into hydrophobic interactions and Van der Waals force which was familiar with former study. Moreover, inhibitor 4 inhibited K562 cell line at the $IC_{50}$ value of 1.22 ${\mu}M$ which was 51-67 times more efficient than that for U937 and HL60 cell lines. Inhibitor 4 exhibited the cell cycle-arrested capability to leukemia at S phase or G2/M phase as well as apoptosis-induced ability in different degrees. Finally, we considered that bicyclic tetrapeptide inhibitors were promising inhibitors used in cancer treatment and inhibitor 4 could prevent K562 cell line well from proliferation, arrest cell cycle and induce K562 towards apoptosis to achieve the goals of reversing cancer cells which could become a potential leukemia therapeutic agent in the future.