Summary information and primary citation
- PDB-id
-
1ngo;
DSSR-derived features in text and
JSON formats
- Class
- DNA
- Method
- NMR
- Summary
- NMR structure of putative 3' terminator for b.
anthracis paga gene coding strand
- Reference
-
Shiflett PR, Taylor-McCabe KJ, Michalczyk R, Silks LA,
Gupta G (2003): "Structural
Studies on the Hairpins at the 3' Untranslated Region of
an Anthrax Toxin Gene." Biochemistry,
42, 6078-6089. doi: 10.1021/bi034128f.
- Abstract
- Three proteins, namely, protective antigen (PA), edema
factor (EF), and lethal factor (LF), encoded by the pX01
plasmid of Bacillus anthracis play a major role in the
pathogenesis of target host cells. PA combines with EF and
LF to form bipartite PA-EF and PA-LF toxins and facilitates
intracellular delivery of EF and LF both of which cause
cytotoxicity to the host. Since the level of PA is crucial
to pathogenesis by anthrax toxins, it is important to
understand how the host environment regulates the
expression of the PA (or pagA) gene by utilizing the 5' and
3' untranslated regions (UTR). The 5' UTR sequence
determines the initiation of transcription, whereas the 3'
UTR sequence determines the efficient termination and
stability of the transcript. Although, the role of the
5'UTR sequence of pagA has been investigated, little is
known about the role of the 3' UTR. Since hairpin formation
at the 3'UTR of a gene is an established mechanism for
efficient termination and stability of the transcript, we
carried out structural studies, including gel
electrophoresis, circular dichroism, and two-dimensional
nuclear magnetic resonance spectroscopy, to determine
whether the 3' UTR sequences of pagA also form hairpin
structures. Our results unequivocally demonstrate that both
the coding and the noncoding 3' UTR sequences form stable
hairpin structures. It is quite likely that the hairpins at
the 3'UTR may contribute to efficient termination and
stability of the pagA transcript.