Structure and Mechanism of the glmS Ribozyme

2008 ◽  
pp. 129-143 ◽  
Author(s):  
Juliane K. Soukup ◽  
Garrett A. Soukup
Keyword(s):  
Glms Ribozyme

scholarly journals In vitro evolution of coenzyme-independent variants from the glmS ribozyme structural scaffold

Methods ◽  
2016 ◽  
Vol 106 ◽  
pp. 76-81 ◽  
Author(s):  
Matthew W.L. Lau ◽  
Adrian R. Ferré-D’Amaré
Keyword(s):  
In Vitro Evolution ◽  
Glms Ribozyme

scholarly journals Measuring the Dimensions of a Compact Kinetic Intermediate in the Folding Pathway of the GlmS Ribozyme

2011 ◽  
Vol 100 (3) ◽  
pp. 237a
Author(s):  
Steve Meisburger ◽  
Krista Brooks ◽  
Suzette Pabit ◽  
Li Li ◽  
Joshua Blose ◽  
...  
Keyword(s):  
Folding Pathway ◽  
Glms Ribozyme ◽  
Kinetic Intermediate

scholarly journals Comprehensive sequence-to-function mapping of cofactor-dependent RNA catalysis in the glmS ribozyme

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Johan O. L. Andreasson ◽  
Andrew Savinov ◽  
Steven M. Block ◽  
William J. Greenleaf
Keyword(s):  
Rna Catalysis ◽  
Glms Ribozyme ◽  
Function Mapping

scholarly journals Ligand Requirements for glmS Ribozyme Self-Cleavage

2005 ◽  
Vol 12 (11) ◽  
pp. 1221-1226 ◽  
Author(s):  
Tom J. McCarthy ◽  
Melissa A. Plog ◽  
Shennen A. Floy ◽  
Joshua A. Jansen ◽  
Juliane K. Soukup ◽  
...  
Keyword(s):  
Glms Ribozyme

scholarly journals Analysis of Metal Ion Dependence in glmS Ribozyme Self-Cleavage and Coenzyme Binding

ChemBioChem ◽  
2010 ◽  
Vol 11 (18) ◽  
pp. 2567-2571 ◽  
Author(s):  
Kevin Klawuhn ◽  
Joshua A. Jansen ◽  
Joshua Souchek ◽  
Garrett A. Soukup ◽  
Juliane K. Soukup
Keyword(s):  
Metal Ion ◽  
Coenzyme Binding ◽  
Glms Ribozyme

scholarly journals An in vitro evolved glmS ribozyme has the wild-type fold but loses coenzyme dependence

2013 ◽  
Vol 9 (12) ◽  
pp. 805-810 ◽  
Author(s):  
Matthew W L Lau ◽  
Adrian R Ferré-D'Amaré
Keyword(s):  
Wild Type ◽  
Glms Ribozyme

scholarly journals Protein abundance and folding rather than the redox state of Kelch13 determine the artemisinin susceptibility of Plasmodium falciparum

2021 ◽  
Author(s):  
Robin Schumann ◽  
Eileen Bischoff ◽  
Severina Klaus ◽  
Sophie Möhring ◽  
Julia Flock ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Survival Rates ◽  
Thiol Group ◽  
Redox Properties ◽  
Protein Abundance ◽  
Mutant Selection ◽  
Redox Sensor ◽  
Glms Ribozyme ◽  
Common Field ◽  
Native Fold

Decreased susceptibilities of Plasmodium falciparum towards the endoperoxide antimalarial artemisinin are linked to mutations of residue C580 of Kelch13, which is the homologue of the redox sensor Keap1 in vertebrates. Here, we addressed whether mutations alter the artemisinin susceptibility by modifying the redox properties of Kelch13 or by compromising its native fold or abundance. Using selection-linked integration and the glmS ribozyme, efficient down-regulation of Kelch13 resulted in ring-stage survival rates around 40%. While the loss of a potential disulfide bond between residues C580 and C532 had no effect on the artemisinin suceptibility, the thiol group of C473 could not be replaced. We also established a protocol for the production of recombinant Kelch13. In contrast to cysteine-to-serine replacements, common field mutations resulted in misfolded and insoluble protein. In summary, not the redox properties but impaired folding of Kelch13, resulting in a decreased Kelch13 abundance, is the central parameter for mutant selection.

scholarly journals Role of the Cofactor in the Catalytic Mechanism of the glmS Ribozyme

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Julia Viladoms Claverol ◽  
Martha J. Fedor
Keyword(s):  
Catalytic Mechanism ◽  
Glms Ribozyme
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