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<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">Dear Pedro, Youri and all,<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">Thank you Youri for the inspiring New Year lecture, and Pedro for the summary of highlights.<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">It is indeed important and fascinating research that points to the evolution of information processing mechanisms in living systems, from ribosomes
to cells and multi-cellular organisms. This research makes an important step towards connecting information processing in the abiotic systems with the one in biological ones.<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">For those of us who are not biologists, it would be good to understand the role of those structures in information processing.<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">Also of relevance might be their temporal behavior, i.e. information transformation and synchronization between processes, including different
levels of organization. Moreover, one would like to make evolutionary connections between those structures and processes on different scales.<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">If I understand correctly, those are open questions. Are there any ideas about answers already?<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US"><o:p> </o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">All the best,<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US">Gordana<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="EN-US" style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US"><o:p> </o:p></span></p>
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<p class="MsoNormal"><span style="font-size:8.0pt;font-family:"Avenir Light",sans-serif;color:black"><a href="http://gordana.se/" title="http://gordana.se/"><span style="color:#0563C1">http://gordana.se/</span></a><o:p></o:p></span></p>
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<p class="MsoNormal"><span style="font-size:11.0pt;font-family:"Avenir Book";mso-fareast-language:EN-US"><o:p> </o:p></span></p>
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<p class="MsoNormal"><b><span style="color:black">From: </span></b><span style="color:black">Fis <fis-bounces@listas.unizar.es> on behalf of "Pedro C. Marijuán" <pedroc.marijuan@gmail.com><br>
<b>Date: </b>Monday, 10 January 2022 at 18:58<br>
<b>To: </b>"fis@listas.unizar.es" <fis@listas.unizar.es><br>
<b>Subject: </b>Re: [Fis] NEW YEAR LECTURE (Youri Timsit)<o:p></o:p></span></p>
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<p class="MsoNormal"><span style="font-size:11.0pt"><o:p> </o:p></span></p>
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<p class="MsoNormal">Dear Youri and colleagues,<o:p></o:p></p>
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<p class="MsoNormal"><o:p> </o:p></p>
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<p class="MsoNormal">Many thanks for your contribution, which we appreciate as it comes from one of the leading groups in ribosome research.
<o:p></o:p></p>
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<p class="MsoNormal">I assume that for some fis parties this kind of cutting edge research may be outside their scope, but it contains a trove of informational problems.<o:p></o:p></p>
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<p class="MsoNormal">And it may deserve an attention effort.<o:p></o:p></p>
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<p class="MsoNormal"><o:p> </o:p></p>
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<p class="MsoNormal">To understand better what I mean, and the full implications of Youri's research, let me recommend his recent paper:<o:p></o:p></p>
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<p class="MsoNormal"><span style="font-size:10.0pt;font-family:Times">Timsit, Y. & Grégoire, S.-P. Towards the Idea of Molecular Brains.
<i>International Journal of Molecular Sciences</i> <b>22</b>, 11868 (2021).</span><o:p></o:p></p>
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<p class="MsoNormal">It is in an open source journal, can be easily downloaded at:
<a href="https://eur01.safelinks.protection.outlook.com/?url=https%3A%2F%2Fwww.mdpi.com%2F1422-0067%2F22%2F21%2F11868&data=04%7C01%7Cgordana.dodig-crnkovic%40mdh.se%7Cade07b6d925d4d3ff52308d9d4628520%7Ca1795b64dabd4758b988b309292316cf%7C0%7C0%7C637774343002525736%7CUnknown%7CTWFpbGZsb3d8eyJWIjoiMC4wLjAwMDAiLCJQIjoiV2luMzIiLCJBTiI6Ik1haWwiLCJXVCI6Mn0%3D%7C2000&sdata=WBtQ1o7933ReviLgj2bCYJ1TNGjj6NbrkKl6%2B0z3yCo%3D&reserved=0">
https://www.mdpi.com/1422-0067/22/21/11868</a><o:p></o:p></p>
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<p class="MsoNormal"><o:p> </o:p></p>
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<p class="MsoNormal">To summarize: we find an amazing protein network in the ribosome,<o:p></o:p></p>
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<p class="MsoNormal">We find an amazing signaling network in eukaryotic cells (and in many prokaryotes too),<o:p></o:p></p>
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<p class="MsoNormal">and we find neuronal networks in primitive nervous systems and also (far more developed) in central nervous systems.<o:p></o:p></p>
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<p class="MsoNormal">These are the main parts of that article (by the way, it contains one of the most cogent compilations of cellular signaling systems--highly recommended only for that).<o:p></o:p></p>
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<p class="MsoNormal"><o:p> </o:p></p>
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<p class="MsoNormal">So, we have three modalities of information processing networks at increasing levels of complexity.<o:p></o:p></p>
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<p class="MsoNormal">The three of them are closely related to "function" of a larger entity, they are "anticipative", and probably can be partially capture by notions of the "Bayesian Brain".
<o:p></o:p></p>
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<p class="MsoNormal"><o:p> </o:p></p>
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<p class="MsoNormal">I have argued several times about the link between signaling systems and the life cycle as the biological underpinnings of "meaning".<o:p></o:p></p>
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<p class="MsoNormal">This is an excellent occasion to realize the full extension of the molecular partners involved.
<o:p></o:p></p>
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<p class="MsoNormal"><o:p> </o:p></p>
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<p class="MsoNormal">Best wishes to all,<o:p></o:p></p>
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<p class="MsoNormal">--Pedro<o:p></o:p></p>
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<p class="MsoNormal"><o:p> </o:p></p>
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<div>
<p class="MsoNormal">El 08/01/2022 a las 20:49, Pedro C. Marijuan escribió:<o:p></o:p></p>
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<p class="MsoNormal" align="right" style="text-align:right"><b>Asunto: <o:p></o:p></b></p>
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<td style="padding:0cm 0cm 0cm 0cm">
<p class="MsoNormal"> NEW YEAR LECTURE<o:p></o:p></p>
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<p class="MsoNormal" align="right" style="text-align:right"><b>Fecha: <o:p></o:p></b></p>
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<p class="MsoNormal">Thu, 06 Jan 2022 15:09:26 +0100<o:p></o:p></p>
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<p class="MsoNormal" align="right" style="text-align:right"><b>De: <o:p></o:p></b></p>
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<td style="padding:0cm 0cm 0cm 0cm">
<p class="MsoNormal">Youri Timsit <a href="mailto:youri.timsit@mio.osupytheas.fr">
<youri.timsit@mio.osupytheas.fr></a><o:p></o:p></p>
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<p class="MsoNormal" align="right" style="text-align:right"><b>Para: <o:p></o:p></b></p>
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<td style="padding:0cm 0cm 0cm 0cm">
<p class="MsoNormal">Pedro C. Marijuán <a href="mailto:pedroc.marijuan@gmail.com">
<pedroc.marijuan@gmail.com></a><o:p></o:p></p>
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<p class="MsoNormal"><span style="color:white"><br>
</span><br>
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<span style="font-size:11.0pt"><o:p></o:p></span></p>
<div>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">Happy New Year to all!
</span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><br>
<br>
<o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">First of all I would like to warmly thank Pedro Marijuán for having offered me to contribute to this New Year lecture.
It is a great pleasure to exchange ideas in a context where “informational choreography”
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">1</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> allows for imaginary encounters between Isadora Duncan and José Ortega y Gasset, to explore
new ways of thinking about “what is life”. The topic of this new year lecture is “molecular brains”, a theme that has recently been developed on the basis of recent work on the ribosome
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">2</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">, D. Bray's seminal paper published in 1995
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">3</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> and the recent papers about consciousness in non-neural organisms </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">4</span></sup><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">Are “molecular brains” a “vision of the mind” or a real property of matter and universe, born from the first forms
of life? And as a corollary, did LUCA have a brain (molecular) and was he “intelligent”? And to go even further, is having systems capable of developing complex behaviours and cognitive faculties a fundamental property of living beings across scales? I hope
that future works will shed light on these questions, but in the meantime, I present here briefly, the elements that led to the conclusion that systems equivalent of “neural networks” on a molecular scale could exist in the ribosome and that these systems
most probably existed before the radiation of the three kingdoms. </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">The ribosome is indeed considered as window towards the earliest forms of life that predate the three kingdoms. While
in astrophysics looking far away gives the opportunity to glimpse the fossil radiation of the universe, looking into the heart of the ribosome may tell us of what the first forms of life might have looked like. The ribosome evolved by accretion around a core
that predates the radiation of the three kingdoms and were probably present in LUCA
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">5–9</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. The ribosomes are thus considered as a relic of ancient translation systems that co-evolved
with the genetic code have evolved by the accretion of rRNA and ribosomal (r)-proteins around a universal core
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">8,10–14</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. They then followed distinct evolutionary pathways to form the bacterial, archaeal
and eukaryotic ribosomes whose overall structures are well conserved within kingdoms
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">15–18</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. The complexity of ribosome assemblies, structures, efficiencies and translation
fidelity concomitantly increased in course of the evolution. </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">The molecular brain’s story started with an attempt to understand the surprising electrostatic properties of the
bL20 ribosomal protein (r-protein), a protein essential for the assembly of the large subunit of the bacterial ribosome
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">19</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. This r-protein had a kind of subversive and unique behaviour in deciding to crystallize
in both a folded and an unfolded form within the same crystal </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">20</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. In trying to better
understand its properties, we compared it to the other r-proteins located in the first high-resolution ribosome structures that had just been published
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">21</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">... and that's when something strange was noticed: we realized that uL13 and uL3, two
r-proteins of the large subunit, were touching each other by a tenuous interaction between their two extensions, long filaments that weave between the phosphate groups of the rRNA. At that time, these famous r-protein extensions were a real enigma. It was
thought that they could play a role in ribosome assembly by neutralising RNA phosphates with their positively charged amino acids
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">22</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. But gradually it became apparent that all extensions of r-proteins systematically wove
a gigantic network based on tiny interactions between them. In general, when proteins interact with partners, they form large interfaces (> 2000 Å<sup>2</sup>) sufficient to stabilise their interactions. In this case, the vast majority of the interfaces did
not exceed 200 Å<sup>2</sup>, which is all the more surprising given that they were extremely conserved phylogenetically
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">23</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">.
</span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">Strikingly, it was found that the r-protein network also interacted with or “innervate” the ribosome functional centres such as tRNA sites, the Peptidyl Transfer Centre (PTC), and
the peptide tunnel </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">23,24</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. Due to its functional analogy with a sensor-motor network, the
r-protein network has been compared to a neural network, at the molecular level. Thus, it has been concluded that these tiny but highly conserved interfaces have been selected during evolution to play a specific role in inter-protein communication and they
possess interacting residues to ensure information transfer from a protein to another. Thus, these tiny “molecular synapses" display a “necessary minimum” for allosteric transmission: a few conserved aromatic/charged amino acid motifs (fig. 1). Moreover, it
is possible that these minimalist “molecular synapses” reveal much more general principles in molecular communication. Indeed, these tiny interfaces, which appear in their simplest expression in the ribosome thanks to the spatial constraints of ribosomal RNA
(rRNA), could be ubiquitous in macromolecular complexes, but drowned out by a 'structural' background involving other amino acids for their stabilisation.
</span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<br>
<br>
<o:p></o:p></p>
<p class="MsoNormal" style="margin-bottom:12.0pt;text-autospace:none"><span style="font-size:8.0pt;font-family:Times">Figure 1. Molecular synapses and wires in the bacterial large subunit r-protein network. The tiny interfaces (the molecular synapses) between
r-proteins are represented by surfaces </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">Data from the literature support our “vision of mind” that r-protein networks could contribute in both the ribosomal assembly and in the “sensorimotor control” during protein synthesis.
Many experimental studies have indeed shown indeed that ribosome functional sites continually exchange and integrate information during the various steps of translation. As the numerous studies of the Dinman group have shown: “<i>an extensive network of information
flow through the ribosome</i>” during protein biosynthesis </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">25–32</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. For example, several
studies have also demonstrated long-range signalling between the decoding centre that monitors the correct geometry of the codon-anticodon and other distant sites such as the Sarcin Ricin Loop (SRL) or the E-tRNA site
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">15,33</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. R-proteins of the ribosomal tunnel also play an active role in the regulation of
protein synthesis and co-translational folding </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">34,35</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. Ribosomes also perceive each other
through quality sensor of collided ribosomes in eukaryotes </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">36</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. In addition, the ribosomes
synchronize many complex movements during the translation cycles </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">37–39</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. The recent discoveries
of “ribosome heterogeneity” </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">40</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> also significantly expands the complexity of the possible
ribosome’s network topologies </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">41</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> and open new perspective on “network plasticity” that
could also play a role its behavioural richness. </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">A recent interdisciplinary study with my mathematician colleagues Daniel Bennequin and Grégoire Segeant-Perthuis has shown how r-protein networks have evolved toward a growing complexity
through the coevolution of the r-protein extensions and the increasing number of connexions
</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">42</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. This study revealed that network expansion is produced by the collective (co)-evolution
of r-proteins leading to an asymmetrical evolution of the two subunits. Furthermore, graph theory showed that the network evolution did not occur at random: each new occurring extensions and connections gradually relates functional modules and places the functional
centres in central positions of the network. The strong selective pressure that is also expressed at the amino acid acquisition links the network architectures and the r-protein phylogeny thus suggesting that the networks have gradually evolved to sophisticated
allosteric pathways. The congruence between independent evolutionary traits indicates that the network architectures evolved to relate and optimize the information spread between functional modules (fig. 2). In summary, graph theory, without knowing the function
of the ribosome, can blindly detect the central functional centres of the ribosome. Conversely, ribosomes have learned graph theory during evolution, by placing the PTC and important functional centres at nodes corresponding to the maximum centrality of the
network.</span><o:p></o:p></p>
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<p class="MsoNormal" style="margin-bottom:12.0pt;text-autospace:none"><b><span style="font-size:8.0pt;font-family:Times">Figure 2. r-protein and functional centres networks in the large subunit of the eukaryotic ribosome.
</span></b><span style="font-size:8.0pt;font-family:Times">The r-proteins and their extensions are represented according to their evolutionary status. Universal (common to bacteria, archaea and eukarya): red; Archaea: cyan; Eukarya: yellow. Lines between two
circles symbolize an interaction between two globular domains. The colours of the lines follow the code for the evolutionary status described above, except for eukarya specific connection that are represented with black lines, for clarity. “N” or “C” indicate
if the seg or mix are N-terminal or C-terminal extensions. NC indicates proteins without a globular domain (uS14, eL29, eS30, eL37 and eL39). Functional sites (PTC, Tunnel, tRNAs and mRNA) are represented in light blue. The names of bacterial proteins which,
by convergence, occupy a position similar to that of Eukaryotic or Archaeal r-proteins, are shown in blue below the circles.
</span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times"> </span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">Moreover, a network archaeology study has also revealed the existence of a universal network, that consists of 49 strictly conserved connections that was probably present before
the radiation of the bacteria and archaea </span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">43</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">. This primordial network is much more developed
in the small ribosomal subunit suggesting that the large subunit network complexity developed in later evolutionary stages. These findings therefore suggest that LUCA already possessed such type of molecular networks, with long wires and tiny interfaces. Interestingly,
these networks also mix the i-systems of rRNA and aromatic amino acids of proteins for forming conserved structural motifs probably involved in a still unknown mechanism of signal transduction (probably involving electron or charge transfer). It is therefore
possible that this ancestral mode of communication has then not only evolved in modern ribosomes but in other macromolecular systems for information transfer and processing. These results therefore suggest that the ribosome opens a window on the first information
processing networks, which appeared at the origin of life. They probably diverged towards other cell systems that have been compared to brains such as the multiple nano-brains. These works provide the molecular basis to decipher how non-neural unicellular
organisms may display complex behaviours such as associative learning and decision-making</span><sup><span style="font-size:10.0pt;line-height:150%;font-family:Times">1,2,44</span></sup><span lang="EN-GB" style="font-size:10.0pt;line-height:150%;font-family:Times">.</span><o:p></o:p></p>
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<span style="font-size:10.0pt;line-height:150%">Waiting for your comments and opinions,</span><o:p></o:p></p>
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<span style="font-size:10.0pt;line-height:150%">Best regards to all!</span><o:p></o:p></p>
<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:150%">
<span style="font-size:10.0pt;line-height:150%">Youri<br>
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<o:p> </o:p></p>
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<pre>_______________________________________________<o:p></o:p></pre>
<pre>Fis mailing list<o:p></o:p></pre>
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<pre>INFORMACIÓN SOBRE PROTECCIÓN DE DATOS DE CARÁCTER PERSONAL<o:p></o:p></pre>
<pre><o:p> </o:p></pre>
<pre>Ud. recibe este correo por pertenecer a una lista de correo gestionada por la Universidad de Zaragoza.<o:p></o:p></pre>
<pre>Puede encontrar toda la información sobre como tratamos sus datos en el siguiente enlace: <a href="https://eur01.safelinks.protection.outlook.com/?url=https%3A%2F%2Fsicuz.unizar.es%2Finformacion-sobre-proteccion-de-datos-de-caracter-personal-en-listas&data=04%7C01%7Cgordana.dodig-crnkovic%40mdh.se%7Cade07b6d925d4d3ff52308d9d4628520%7Ca1795b64dabd4758b988b309292316cf%7C0%7C0%7C637774343002525736%7CUnknown%7CTWFpbGZsb3d8eyJWIjoiMC4wLjAwMDAiLCJQIjoiV2luMzIiLCJBTiI6Ik1haWwiLCJXVCI6Mn0%3D%7C2000&sdata=eoeUfDwkyZ5732%2BJZrYXL963Ymm4KupM5nZMzlaFHmE%3D&reserved=0">https://sicuz.unizar.es/informacion-sobre-proteccion-de-datos-de-caracter-personal-en-listas</a><o:p></o:p></pre>
<pre>Recuerde que si está suscrito a una lista voluntaria Ud. puede darse de baja desde la propia aplicación en el momento en que lo desee.<o:p></o:p></pre>
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