FN Archimer Export Format
PT J
TI Convergent Evolution and Structural Adaptation to the Deep Ocean in the Protein-Folding Chaperonin CCTα
BT 
AF Weber, Alexandra AT
   Hugall, Andrew F
   O’Hara, Timothy D
AS 1:1,2,3;2:1;3:1;
FF 1:PDG-REM-EEP-LEP;2:;3:;
C1 Sciences, Museums Victoria, Melbourne, Victoria, Australia
   Centre de Bretagne, REM/EEP, Ifremer, Laboratoire Environnement Profond, Plouzané, France
   Zoological Institute, University of Basel, Switzerland
C2 MUSEUMS VICTORIA, AUSTRALIA
   IFREMER, FRANCE
   UNIV BASEL, SWITZERLAND
SI BREST
SE PDG-REM-EEP-LEP
IN WOS Ifremer UPR
   DOAJ
   copubli-int-hors-europe
IF 3.416
TC 7
UR https://archimer.ifremer.fr/doc/00659/77136/78452.pdf
   https://archimer.ifremer.fr/doc/00659/77136/78453.zip
LA English
DT Article
DE ;Echinodermata;TC P-1;protein folding;positive selection;protein stability;pressure adaptation
AB The deep ocean is the largest biome on Earth and yet it is among the least studied environments of our planet. Life at great depths requires several specific adaptations; however, their molecular mechanisms remain understudied. We examined patterns of positive selection in 416 genes from four brittle star (Ophiuroidea) families displaying replicated events of deep-sea colonization (288 individuals from 216 species). We found consistent signatures of molecular convergence in functions related to protein biogenesis, including protein folding and translation. Five genes were recurrently positively selected, including chaperonin-containing TCP-1 subunit α (CCTα), which is essential for protein folding. Molecular convergence was detected at the functional and gene levels but not at the amino-acid level. Pressure-adapted proteins are expected to display higher stability to counteract the effects of denaturation. We thus examined in silico local protein stability of CCTα across the ophiuroid tree of life (967 individuals from 725 species) in a phylogenetically corrected context and found that deep-sea-adapted proteins display higher stability within and next to the substrate-binding region, which was confirmed by in silico global protein stability analyses. This suggests that CCTα displays not only structural but also functional adaptations to deep-water conditions. The CCT complex is involved in the folding of ∼10% of newly synthesized proteins and has previously been categorized as a “cold-shock” protein in numerous eukaryotes. We thus propose that adaptation mechanisms to cold and deep-sea environments may be linked and highlight that efficient protein biogenesis, including protein folding and translation, is a key metabolic deep-sea adaptation. 
PY 2020
PD NOV
SO Genome Biology And Evolution
SN 1759-6653
PU Oxford University Press (OUP)
VL 12
IS 11
UT 000599652700001
BP 1929
EP 1942
DI 10.1093/gbe/evaa167
ID 77136
ER

EF