Next Article in Journal
Unveiling the Molecular Basis of the Noonan Syndrome-Causing Mutation T42A of SHP2
Previous Article in Journal
Supporting Cell-Based Tendon Therapy: Effect of PDGF-BB and Ascorbic Acid on Rabbit Achilles Tenocytes In Vitro
Article

Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes

1
Institute for Biochemistry, Leipzig University, Brüderstraße 34, 04103 Leipzig, Germany
2
Computational EvoDevo Group, Department of Computer Science, Leipzig University, Härtelstraße 16-18, 04107 Leipzig, Germany
3
Interdisciplinary Center for Bioinformatics, Leipzig University, Härtelstraße 16-18, 04107 Leipzig, Germany
4
Santa Fe Institute for Complex Systems, 1399 Hyde Park Road, Santa Fe, NM 87501, USA
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2020, 21(2), 462; https://doi.org/10.3390/ijms21020462
Received: 20 December 2019 / Revised: 6 January 2020 / Accepted: 9 January 2020 / Published: 10 January 2020
(This article belongs to the Section Molecular Biology)
Synthesis of the CCA end of essential tRNAs is performed either by CCA-adding enzymes or as a collaboration between enzymes restricted to CC- and A-incorporation. While the occurrence of such tRNA nucleotidyltransferases with partial activities seemed to be restricted to Bacteria, the first example of such split CCA-adding activities was reported in Schizosaccharomyces pombe. Here, we demonstrate that the choanoflagellate Salpingoeca rosetta also carries CC- and A-adding enzymes. However, these enzymes have distinct evolutionary origins. Furthermore, the restricted activity of the eukaryotic CC-adding enzymes has evolved in a different way compared to their bacterial counterparts. Yet, the molecular basis is very similar, as highly conserved positions within a catalytically important flexible loop region are missing in the CC-adding enzymes. For both the CC-adding enzymes from S. rosetta as well as S. pombe, introduction of the loop elements from closely related enzymes with full activity was able to restore CCA-addition, corroborating the significance of this loop in the evolution of bacterial as well as eukaryotic tRNA nucleotidyltransferases. Our data demonstrate that partial CC- and A-adding activities in Bacteria and Eukaryotes are based on the same mechanistic principles but, surprisingly, originate from different evolutionary events. View Full-Text
Keywords: tRNA nucleotidyltransferase; enzyme evolution; Salpingoeca rosetta; Schizosaccharomyces pombe tRNA nucleotidyltransferase; enzyme evolution; Salpingoeca rosetta; Schizosaccharomyces pombe
Show Figures

Figure 1

MDPI and ACS Style

Erber, L.; Franz, P.; Betat, H.; Prohaska, S.; Mörl, M. Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes. Int. J. Mol. Sci. 2020, 21, 462. https://doi.org/10.3390/ijms21020462

AMA Style

Erber L, Franz P, Betat H, Prohaska S, Mörl M. Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes. International Journal of Molecular Sciences. 2020; 21(2):462. https://doi.org/10.3390/ijms21020462

Chicago/Turabian Style

Erber, Lieselotte, Paul Franz, Heike Betat, Sonja Prohaska, and Mario Mörl. 2020. "Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes" International Journal of Molecular Sciences 21, no. 2: 462. https://doi.org/10.3390/ijms21020462

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop