scholarly journals Elena Gracheva: Ion channels run hot and cold

2015 ◽  
Vol 209 (6) ◽  
pp. 778-779 ◽  
Author(s):  
Caitlin Sedwick

Gracheva studies the molecular basis and evolutionary origins of hibernation.

Archaea ◽  
2002 ◽  
Vol 1 (1) ◽  
pp. 35-44 ◽  
Author(s):  
Anna Kloda ◽  
Boris Martinac

The ubiquity of mechanosensitive (MS) channels triggered a search for their functional homologs in Archaea. Archaeal MS channels were found to share a common ancestral origin with bacterial MS channels of large and small conductance, and sequence homology with several proteins that most likely function as MS ion channels in prokaryotic and eukaryotic cell-walled organisms. Although bacterial and archaeal MS channels differ in conductive and mechanosensitive properties, they share similar gating mechanisms triggered by mechanical force transmitted via the lipid bilayer. In this review, we suggest that MS channels of Archaea can bridge the evolutionary gap between bacterial and eukaryotic MS channels, and that MS channels of Bacteria, Archaea and cell-walled Eukarya may serve similar physiological functions and may have evolved to protect the fragile cellular membranes in these organisms from excessive dilation and rupture upon osmotic challenge.


2017 ◽  
Vol 112 (3) ◽  
pp. 420a
Author(s):  
Timothy Lynagh ◽  
Jose L. Romero-Rojo ◽  
Stephan A. Pless

2020 ◽  
Vol 21 (2) ◽  
pp. 462 ◽  
Author(s):  
Lieselotte Erber ◽  
Paul Franz ◽  
Heike Betat ◽  
Sonja Prohaska ◽  
Mario Mörl

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.


2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Lei Luo ◽  
Yunfei Wang ◽  
Bowen Li ◽  
Lizhen Xu ◽  
Peter Muiruri Kamau ◽  
...  
Keyword(s):  

2019 ◽  
Vol 116 (3) ◽  
pp. 110a
Author(s):  
Zeshan P. Sheikh ◽  
Timothy Lynagh ◽  
Emelie Flood ◽  
Celine Boiteux ◽  
Toby W. Allen ◽  
...  

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Timothy Lynagh ◽  
Robin N. Beech ◽  
Maryline J. Lalande ◽  
Kevin Keller ◽  
Brett A. Cromer ◽  
...  

1993 ◽  
Vol 72 (3) ◽  
pp. 491-496 ◽  
Author(s):  
G F Tomaselli ◽  
P H Backx ◽  
E Marban

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