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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>
Diversity and Polymorphism in AHL-Lactonase Gene (aiiA) of Bacillus
( Huma Nusrat ),( Pratap Shankar ),( Jyoti Kushwah ),( Ashish Bhushan ),( Jayadev Joshi ),( Tanmoy Mukherjee ),( Sajan C. Raju ),( Hemant J. Purohit ),( Vipin Chandra Kalia ) 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.10
To explore bacterial diversity for elucidating genetic variability in acylhomoserine lactone (AHL) lactonase structure, we screened 800 bacterial strains. It revealed the presence of a quorum quenching (QQ) AHL-lactonase gene (aiiA) in 42 strains. These 42 strains were identified using rrs (16S rDNA) sequencing as Bacillus strains, predominantly B. cereus. An in silico restriction endonuclease (RE) digestion of 22 AHL lactonase gene (aiiA) sequences (from NCBI database) belonging to 9 different genera, along with 42 aiiA gene sequences from different Bacillus spp. (isolated here) with 14 type II REs, revealed distinct patterns of fragments (nucleotide length and order) with four REs; AluI, DpnII, RsaI, and Tru9I. Our study reflects on the biodiversity of aiiA among Bacillus species. Bacillus sp. strain MBG11 with polymorphism (115Alanine > Valine) may confer increased stability to AHL lactonase, and can be a potential candidate for heterologous expression and mass production. Microbes with ability to produce AHL-lactonases degrade quorum sensing signals such as AHL by opening of the lactone ring. The naturally occurring diversity of QQ molecules provides opportunities to use them for preventing bacterial infections, spoilage of food, and bioremediation.