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- 저자 : Bothra, Shilpa (검색결과 2 건)
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Kim, Gi-Dong,Bothra, Shilpa,Sahoo, Suban K.,Choi, Heung-Jin Elsevier 2018 Tetrahedron letters: the international organ for t Vol.59 No.17
<P><B>Abstract</B></P> <P>To avoid the deprotonation events occurred in the receptor upon recognition of basic anions, a novel <I>C<SUB>3v</SUB> </I>-symmetric anion receptor <B>2</B> with two amide groups appended in each arm was designed and synthesized by using the trindane tricarboxylic acid as tripodal molecular framework. The anion recognition ability by <B>2</B> was examined by <SUP>1</SUP>H NMR titration study in DMSO-<I>d</I> <SUB>6</SUB>, which revealed that the addition of H<SUB>2</SUB>PO<SUB>4</SUB> <SUP>−</SUP> guests caused substantial downfield shifts of the amide-NH protons peaks due to the formation of a host-guest complex in 1:1 binding stoichiometry with the estimated binding constant (<I>K</I> <SUB>a</SUB>) of 244 M<SUP>−1</SUP>. No noticeable binding of <B>2</B> was observed with other tested anions such as F<SUP>−</SUP>, Cl<SUP>−</SUP>, Br<SUP>−</SUP>, I<SUP>−</SUP>, NO<SUB>3</SUB> <SUP>−</SUP> and HSO<SUB>4</SUB> <SUP>−</SUP> under similar conditions.</P> <P><B>Highlights</B></P> <P> <UL> <LI> A tripodal anion receptor <B>2</B> with three diamide groups on trindane was synthesized. </LI> <LI> The anion recognition ability by <B>2</B> was examined by <SUP>1</SUP>H NMR in DMSO-<I>d</I> <SUB>6</SUB>. </LI> <LI> Addition of H<SUB>2</SUB>PO<SUB>4</SUB> <SUP>−</SUP> guest caused downfield shifts of the amide-NH protons peaks of <B>2</B>. </LI> <LI> Receptor <B>2</B> formed a 1:1 complex with H<SUB>2</SUB>PO<SUB>4</SUB> <SUP>−</SUP> with binding constant (<I>K</I> <SUB>a</SUB>) of 244 M<SUP>−1</SUP>. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
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Virmani, Richa,Sajid, Andaleeb,Singhal, Anshika,Gaur, Mohita,Joshi, Jayadev,Bothra, Ankur,Garg, Richa,Misra, Richa,Singh, Vijay Pal,Molle, Virginie,Goel, Ajay K.,Singh, Archana,Kalia, Vipin C.,Lee, Ju American Society for Biochemistry and Molecular Bi 2019 The Journal of biological chemistry Vol.294 No.22
<P><I>Bacillus anthracis</I> is the causative agent of anthrax in humans, bovine, and other animals. <I>B. anthracis</I> pathogenesis requires differentiation of dormant spores into vegetative cells. The spores inherit cellular components as phenotypic memory from the parent cell, and this memory plays a critical role in facilitating the spores' revival. Because metabolism initiates at the beginning of spore germination, here we metabolically reprogrammed <I>B. anthracis</I> cells to understand the role of glycolytic enzymes in this process. We show that increased expression of enolase (Eno) in the sporulating mother cell decreases germination efficiency. Eno is phosphorylated by the conserved Ser/Thr protein kinase PrkC which decreases the catalytic activity of Eno. We found that phosphorylation also regulates Eno expression and localization, thereby controlling the overall spore germination process. Using MS analysis, we identified the sites of phosphorylation in Eno, and substitution(s) of selected phosphorylation sites helped establish the functional correlation between phosphorylation and Eno activity. We propose that PrkC-mediated regulation of Eno may help sporulating <I>B. anthracis</I> cells in adapting to nutrient deprivation. In summary, to the best of our knowledge, our study provides the first evidence that in sporulating <I>B. anthracis</I>, PrkC imprints phenotypic memory that facilitates the germination process.</P>
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