Dataset Information


Cold adaptation of tRNA nucleotidyltransferases: a tradeoff in activity, stability and fidelity

ABSTRACT: CCA-adding enzymes are highly specific RNA polymerases that synthesize and maintain the sequence CCA at the tRNA 3‘-end. Here, we investigated the impact of cold adaptation on the reactivity and specificity of CCA-adding enzymes from psychrophilic bacteria. A comparative study of the corresponding enzymes from closely related psychro-, meso-, and thermophilic Bacillales indicates that the cold-adapted enzymes show a considerable error rate during CCA synthesis, resulting in additional incorporations of C and A residues. It seems that the activity of psychrophilic CCA-adding enzymes is not only achieved at the expense of structural stability, reaction velocity and substrate affinity, but also results in a reduced polymerization fidelity. Overall design: in vivo tRNA from four Bacillales species was isolated from exponential and stationary growth phase each in triplicates resulting in a total of 24 samples. Sequencing libraries were created for small RNA species and sequenced on 3 runs of a MiSeq using 8 indices. Reads were analyzed regarding 3'-ends of tRNA and results summed up as a mean for the 8 conditions investigated. Results from B. subtilis were regarded as reference sample for a mesophilic Bacillales species. Differences towards psychophilic Planococcus halocryophilus and Exiguobacterium sibiricum and thermophilic Geobacills stearothermophilus were investigated.


INSTRUMENT(S): Illumina MiSeq (Planococcus halocryophilus)

SUBMITTER: Felix Georg Maria Ernst 

PROVIDER: GSE98874 | GEO | 2017-11-03



Dataset's files

Action DRS
GSE98874_RAW.tar Raw
filelist.txt Txt
Items per page:
1 - 2 of 2
altmetric image


Cold adaptation of tRNA nucleotidyltransferases: A tradeoff in activity, stability and fidelity.

Ernst Felix G M FGM   Erber Lieselotte L   Sammler Joana J   Jühling Frank F   Betat Heike H   Mörl Mario M  

RNA biology 20171121 1

Cold adaptation is an evolutionary process that has dramatic impact on enzymatic activity. Increased flexibility of the protein structure represents the main evolutionary strategy for efficient catalysis and reaction rates in the cold, but is achieved at the expense of structural stability. This results in a significant activity-stability tradeoff, as it was observed for several metabolic enzymes. In polymerases, however, not only reaction rates, but also fidelity plays an important role, as the  ...[more]

Similar Datasets

2018-01-01 | S-EPMC5785979 | BioStudies
2008-01-01 | S-EPMC2430343 | BioStudies
2011-11-17 | E-GEOD-33756 | ArrayExpress
1000-01-01 | S-EPMC3248509 | BioStudies
2011-01-01 | S-EPMC3273417 | BioStudies
2011-01-01 | S-EPMC3134780 | BioStudies
2003-01-01 | S-EPMC275420 | BioStudies
1000-01-01 | S-EPMC4538823 | BioStudies
2020-01-01 | S-EPMC7014341 | BioStudies
1000-01-01 | S-EPMC1765476 | BioStudies