@article {2016|1746,
	title = {Evolution of Pentameric Ligand-Gated Ion Channels: Pro-Loop Receptors.},
	journal = {Plos One},
	volume = {11},
	year = {2016},
	pages = {e0151934},
	abstract = {<p>Pentameric ligand-gated ion channels (pLGICs) are ubiquitous neurotransmitter receptors in Bilateria, with a small number of known prokaryotic homologues. Here we describe a new inventory and phylogenetic analysis of pLGIC genes across all kingdoms of life. Our main finding is a set of pLGIC genes in unicellular eukaryotes, some of which are metazoan-like Cys-loop receptors, and others devoid of Cys-loop cysteines, like their prokaryotic relatives. A number of such \&quot;Cys-less\&quot; receptors also appears in invertebrate metazoans. Together, those findings draw a new distribution of pLGICs in eukaryotes. A broader distribution of prokaryotic channels also emerges, including a major new archaeal taxon, Thaumarchaeota. More generally, pLGICs now appear nearly ubiquitous in major taxonomic groups except multicellular plants and fungi. However, pLGICs are sparsely present in unicellular taxa, suggesting a high rate of gene loss and a non-essential character, contrasting with their essential role as synaptic receptors of the bilaterian nervous system. Multiple alignments of these highly divergent sequences reveal a small number of conserved residues clustered at the interface between the extracellular and transmembrane domains. Only the \&quot;Cys-loop\&quot; proline is absolutely conserved, suggesting the more fitting name \&quot;Pro loop\&quot; for that motif, and \&quot;Pro-loop receptors\&quot; for the superfamily. The infered molecular phylogeny shows a Cys-loop and a Cys-less clade in eukaryotes, both containing metazoans and unicellular members. This suggests new hypotheses on the evolutionary history of the superfamily, such as a possible origin of the Cys-loop cysteines in an ancient unicellular eukaryote. Deeper phylogenetic relationships remain uncertain, particularly around the split between bacteria, archaea, and eukaryotes.</p>},
	issn = {1932-6203},
	doi = {10.1371/journal.pone.0151934},
	author = {Jaiteh, Mariama and Antoine Taly and J{\'e}r{\^o}me H{\'e}nin}
}
@article {2002|2002,
	title = {{E}ffect of binding of {C}d2+ on bacterial reaction center mutants: proton-transfer uses interdependent pathways},
	journal = {Biochemistry},
	volume = {41},
	number = {29},
	year = {2002},
	month = {jul},
	pages = {9132{\textendash}9138},
	publisher = {ACS Publications},
	author = {Gerencser, L. and Antoine Taly and Baciou, L. and Maroti, P. and Sebban, P.}
}
