期刊
MOLECULAR MICROBIOLOGY
卷 119, 期 6, 页码 711-727出版社
WILEY
DOI: 10.1111/mmi.15066
关键词
Borrelia burgdorferi; c-di-GMP; Lyme disease; PlzA; RNA chaperone
This study found that PlzA protein has RNA chaperone activity, which is inhibited by c-di-GMP binding. PlzA can bind RNA and accelerate RNA annealing, and only apo-PlzA can strand displace and unwind double-stranded RNA. It is proposed that PlzA regulates gene expression during both the vector and host phases of the B. burgdorferi life cycle through complex RNA-mediated mechanisms.
PlzA is a c-di-GMP-binding protein crucial for adaptation of the Lyme disease spirochete Borrelia (Borreliella) burgdorferi during its enzootic life cycle. Unliganded apo-PlzA is important for vertebrate infection, while liganded holo-PlzA is important for survival in the tick; however, the biological function of PlzA has remained enigmatic. Here, we report that PlzA has RNA chaperone activity that is inhibited by c-di-GMP binding. Holo- and apo-PlzA bind RNA and accelerate RNA annealing, while only apo-PlzA can strand displace and unwind double-stranded RNA. Guided by the crystal structure of PlzA, we identified several key aromatic amino acids protruding from the N- and C-terminal domains that are required for RNA-binding and unwinding activity. Our findings illuminate c-di-GMP as a switch controlling the RNA chaperone activity of PlzA, and we propose that complex RNA-mediated modulatory mechanisms allow PlzA to regulate gene expression during both the vector and host phases of the B. burgdorferi life cycle.
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