Abstract
The glmS bacterial ribozyme/riboswitch is found in a number of Gram-positive bacteria, many of which are human pathogens. Investigation of the structure and function of the glmS catalyst will aid in the development of artificial agonists/antagonists that might function as novel antibiotics. The glmS ribozyme is mechanistically unique in that it is the first RNA catalyst identified to require a coenzyme, glucosamine-6-phosphate, for RNA self-cleavage. In addition, it is the first riboswitch identified to utilize self-cleavage as a mode of genetic regulation in metabolism. Significant biochemical and biophysical data exist for the glmS ribozyme and aid in mechanistically understanding the importance of RNA and coenzyme structure to function in acid-base catalysis.
| Original language | English |
|---|---|
| Title of host publication | Catalytic RNA |
| Publisher | Elsevier |
| Pages | 173-193 |
| Number of pages | 21 |
| Volume | 120 |
| ISBN (Print) | 9780123812865 |
| DOIs | |
| State | Published - 2013 |
Publication series
| Name | Progress in Molecular Biology and Translational Science |
|---|---|
| Volume | 120 |
| ISSN (Print) | 18771173 |
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All Science Journal Classification (ASJC) codes
- Molecular Biology
- Molecular Medicine
Cite this
The structural and functional uniqueness of the glmS ribozyme. / Strauss-Soukup, Juliane K.
Catalytic RNA. Vol. 120 Elsevier, 2013. p. 173-193 (Progress in Molecular Biology and Translational Science; Vol. 120).Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - The structural and functional uniqueness of the glmS ribozyme
AU - Strauss-Soukup, Juliane K.
PY - 2013
Y1 - 2013
N2 - The glmS bacterial ribozyme/riboswitch is found in a number of Gram-positive bacteria, many of which are human pathogens. Investigation of the structure and function of the glmS catalyst will aid in the development of artificial agonists/antagonists that might function as novel antibiotics. The glmS ribozyme is mechanistically unique in that it is the first RNA catalyst identified to require a coenzyme, glucosamine-6-phosphate, for RNA self-cleavage. In addition, it is the first riboswitch identified to utilize self-cleavage as a mode of genetic regulation in metabolism. Significant biochemical and biophysical data exist for the glmS ribozyme and aid in mechanistically understanding the importance of RNA and coenzyme structure to function in acid-base catalysis.
AB - The glmS bacterial ribozyme/riboswitch is found in a number of Gram-positive bacteria, many of which are human pathogens. Investigation of the structure and function of the glmS catalyst will aid in the development of artificial agonists/antagonists that might function as novel antibiotics. The glmS ribozyme is mechanistically unique in that it is the first RNA catalyst identified to require a coenzyme, glucosamine-6-phosphate, for RNA self-cleavage. In addition, it is the first riboswitch identified to utilize self-cleavage as a mode of genetic regulation in metabolism. Significant biochemical and biophysical data exist for the glmS ribozyme and aid in mechanistically understanding the importance of RNA and coenzyme structure to function in acid-base catalysis.
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U2 - 10.1016/B978-0-12-381286-5.00005-6
DO - 10.1016/B978-0-12-381286-5.00005-6
M3 - Chapter
C2 - 24156944
AN - SCOPUS:84896697569
SN - 9780123812865
VL - 120
T3 - Progress in Molecular Biology and Translational Science
SP - 173
EP - 193
BT - Catalytic RNA
PB - Elsevier
ER -