[Fis] NEW YEAR LECTURE (Youri Timsit)

[Karl Javorszky]

Dear Colleagues,



It is a great pleasure that the series of Sessions have recommenced, and
namely with such an excellent tour d’horizon. The subsequent contributions
also show great attention to detail and elaborate knowledge of the matter.

Joseph’s story shows that we – as a group – are farther away from the
mainstream as optimal. The messages from the avant-garde should be
understood.

Joe has my full sympathy. The concepts offered here need more explanations,
not because they are not valid, but because the audience is nut fully done
yet with understanding the fundamental duality that underlies the concept.
The words appropriate for the discussion are lacking, because the concepts
that are the subject of the discussion are not yet delineated and
recognised, because the concepts cannot be perceived lacking a background
perspective.



Mendel has suffered the same rebuffs as Joe, among others. Mendel has
pointed out statistical patterns. The implication was that there is
something material within the plant that carries the genetic information.
The words chromosome, genome, triplet weren’t available for the discussion,
because the concepts of common structures in all cells have not yet been
worked out, because the framework of looking for something divine through
the microscope was unthinkable, there being the theoretical, intellectual,
theological level of ideas about progeniture and then there was the level
of things and innate objects. In that age, the fusion of levels of
organised concepts was necessary, as researchers evolved the idea of
“looking for God’s work in the laboratory”.

Today the sea change is into one of separation, division, opposition,
polarisation, incongruence which all appear to us today either as
inexactitude or as God’s mysteries. The more conflicting and only partly
harmonising general world view should and necessarily will replace the
previous view of the world as a unified, harmonised, seamlessly fitting,
contradiction-free contraption. Joe speaks of two systems of concepts –
Logic and Reality -, and how these interact and are interrelated. There has
been research ongoing to some basic problems of information processing,
relating to the two origins of excitation patterns (the actual and the
memorised version), independently of Joseph’s ideas and endorsement. This
research has brought up an uncommon but indisputable fact, that namely
there are *two *interdependent systems in existence, and their interactions
and interrelations are manifold and instructive. Many of the apparent
inexactitudes and God’s mysteries can be explained as the artefact of
having two interrelated systems interacting. Once we count in stereo, we
understand patterns of standing waves. A system of thoughts that is based
on the interaction of two interrelated systems is supported by properties
of natural numbers.

In summary, my encouragement goes to Joe specifically and to all of us
generally. To be not understood is by no means a judgement on the soundness
of one’s ideas, and if the members of one’s club repeatedly remark that
they are not understood then one is in the right kind of club, among people
who think up something new.

Karl

Am Mi., 12. Jan. 2022 um 19:08 Uhr schrieb Loet Leydesdorff <
loet en leydesdorff.net>:

> Dear Gordana:
>
> I highly appreciate your comments. They re to the point.
>
>
> For those of us who are not biologists, it would be good to understand the
> role of those structures in information processing.
>
> Structures are structural and systemic. Unlike variation, they are not
> manifest (phenotypical). They are selective. Selection may change the
> balance between filled and unfilled boxes in the data matrix, and thus
> between entropy and redundancy. [H (max) = R + I)]
>
> Also of relevance might be their temporal behavior, i.e. information
> transformation and synchronization between processes, including different
> levels of organization.
>
> Would this be the dynamic (temporal) equivalent of structures at each
> moment of time?
>
> Moreover, one would like to make evolutionary connections between those
> structures and processes on different scales.
>
> If I understand correctly, those are open questions. Are there any ideas
> about answers already?
>
> The selection mechanisms are probably different. I like this intuition
> from Luhmann (in the discussion with Habermas, 1971):
>
> Rather, what is special about the meaningful or meaning-based processing
> of experience is that it makes possible *both *the reduction and the
> preservation of complexity; i.e., it provides a form of selection that
> prevents the world from shrinking down to just one particular content of
> consciousness with each act of determining experience. (1990, p. 27)
>
> It seems to me that this other selection mechanism would be intentional
> and therefore future oriented, while traditional selection evolves in
> history. A further selection on historical trajectories can lead to
> evolutionary regimes. Trajectories are history-based; regimes
> expectation-based. The Dubois-formulas for anticipation could be helpful
> for the formalization. Biological selection (upon variation) would then be
> a special case or -- in other words -- a subdynamic (retention).
>
> Best, Loet
>
> PS: Happy New Year for all of you! L.
>
> *_______________*
>
> * <https://www.springer.com/gp/book/9783030599508>Loet Leydesdorff*
>
>
> *"The Evolutionary Dynamics of Discusive Knowledge"
> <https://link.springer.com/book/10.1007/978-3-030-59951-5>(Open Access)*
>
> Professor emeritus, University of Amsterdam
>
> Amsterdam School of Communication Research (ASCoR)
>
> loet en leydesdorff.net ; http://www.leydesdorff.net/
>
> http://scholar.google.com/citations?user=ych9gNYAAAAJ&hl=en
>
> ORCID: http://orcid.org/0000-0002-7835-3098;
>
>
>
>
>
>
> All the best,
>
> Gordana
>
>
>
> http://gordana.se/
>
>
>
> *From: *Fis <fis-bounces en listas.unizar.es> on behalf of "Pedro C.
> Marijuán" <pedroc.marijuan en gmail.com>
> *Date: *Monday, 10 January 2022 at 18:58
> *To: *"fis en listas.unizar.es" <fis en listas.unizar.es>
> *Subject: *Re: [Fis] NEW YEAR LECTURE (Youri Timsit)
>
>
>
> Dear Youri and colleagues,
>
>
>
> Many thanks for your contribution, which we appreciate as it comes from
> one of the leading groups in ribosome research.
>
> 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.
>
> And it may deserve an attention effort.
>
>
>
> To understand better what I mean, and the full implications of Youri's
> research, let me recommend his recent paper:
>
> Timsit, Y. & Grégoire, S.-P. Towards the Idea of Molecular Brains. *International
> Journal of Molecular Sciences* *22*, 11868 (2021).
>
> It is in an open source journal, can be easily downloaded at:
> https://www.mdpi.com/1422-0067/22/21/11868
> <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>
>
>
>
> To summarize: we find an amazing protein network in the ribosome,
>
> We find an amazing signaling network in eukaryotic cells (and in many
> prokaryotes too),
>
> and we find neuronal networks in primitive nervous systems and also (far
> more developed) in central nervous systems.
>
> 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).
>
>
>
> So, we have three modalities of information processing networks at
> increasing levels of complexity.
>
> 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".
>
>
>
> I have argued several times about the link between signaling systems and
> the life cycle as the biological underpinnings of "meaning".
>
> This is an excellent occasion to realize the full extension of the
> molecular partners involved.
>
>
>
> Best wishes to all,
>
> --Pedro
>
>
>
> El 08/01/2022 a las 20:49, Pedro C. Marijuan escribió:
>
> *Asunto: *
>
>  NEW YEAR LECTURE
>
> *Fecha: *
>
> Thu, 06 Jan 2022 15:09:26 +0100
>
> *De: *
>
> Youri Timsit <youri.timsit en mio.osupytheas.fr>
> <youri.timsit en mio.osupytheas.fr>
>
> *Para: *
>
> Pedro C. Marijuán <pedroc.marijuan en gmail.com> <pedroc.marijuan en gmail.com>
>
>
>
>
> Happy New Year to all!
>
>
>
> 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” 1
> 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 2,  D. Bray's
> seminal paper published in 1995 3 and the recent papers about
> consciousness in non-neural organisms 4
>
>
>
> 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.
>
>
>
> 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 5–9. 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 8,10–14. They then followed distinct evolutionary pathways
> to form the bacterial, archaeal and eukaryotic ribosomes whose overall
> structures are well conserved within kingdoms 15–18. The complexity of
> ribosome assemblies, structures, efficiencies and translation fidelity
> concomitantly increased in course of the evolution.
>
>
>
> 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 19. 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 20. 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 21...
> 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 22. 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 Å2) sufficient to stabilise
> their interactions. In this case, the vast majority of the interfaces did
> not exceed 200 Å2, which is all the more surprising given that they were
> extremely conserved phylogenetically 23.
>
>
>
> 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 23,24. 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.
>
>
>
> 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
>
>
>
> 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: “*an extensive
> network of information flow through the ribosome*” during protein
> biosynthesis 25–32. 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 15,33. R-proteins of the ribosomal
> tunnel also play an active role in the regulation of protein synthesis and
> co-translational folding 34,35. Ribosomes also perceive each other
> through quality sensor of collided ribosomes in eukaryotes 36. In
> addition, the ribosomes synchronize many complex movements during the
> translation cycles 37–39. The recent discoveries of “ribosome
> heterogeneity” 40 also significantly expands the complexity of the
> possible ribosome’s network topologies 41 and  open new perspective on
> “network plasticity” that could also play a role its behavioural richness.
>
> 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 42. 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.
>
>
>
>
>
> *Figure 2. r-protein and functional centres  networks in the large subunit
> of the eukaryotic ribosome. *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.
>
>
>
> 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 43.
> 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-making1,2,44.
>
>
>
> Waiting for your comments and opinions,
>
> Best regards to all!
>
> Youri
>
>
>
> 1.         Marijuán, P. C., Navarro, J. & del Moral, R. How the living is
> in the world: An inquiry into the informational choreographies of life. *Prog
> Biophys Mol Biol* *119*, 469–480 (2015).
>
> 2.         Timsit, Y. & Grégoire, S.-P. Towards the Idea of Molecular
> Brains. *International Journal of Molecular Sciences* *22*, 11868 (2021).
>
> 3.         Bray, D. Protein molecules as computational elements in living
> cells. *Nature* *376*, 307–312 (1995).
>
> 4.         Baluška, F., Miller, W. B. & Reber, A. S. Biomolecular Basis of
> Cellular Consciousness via Subcellular Nanobrains. *International Journal
> of Molecular Sciences* *22*, 2545 (2021).
>
> 5.         Belousoff, M. J. *et al.* Ancient machinery embedded in the
> contemporary ribosome. *Biochem. Soc. Trans.* *38*, 422–427 (2010).
>
> 6.         Fox, G. E. Origin and evolution of the ribosome. *Cold Spring
> Harb Perspect Biol* *2*, a003483 (2010).
>
> 7.         Opron, K. & Burton, Z. F. Ribosome Structure, Function, and
> Early Evolution. *Int J Mol Sci* *20*, (2018).
>
> 8.         Melnikov, S. *et al.* One core, two shells: bacterial and
> eukaryotic ribosomes. *Nat. Struct. Mol. Biol.* *19*, 560–567 (2012).
>
> 9.         Lecompte, O., Ripp, R., Thierry, J.-C., Moras, D. & Poch, O.
> Comparative analysis of ribosomal proteins in complete genomes: an example
> of reductive evolution at the domain scale. *Nucleic Acids Res.* *30*,
> 5382–5390 (2002).
>
> 10.        Petrov, A. S. *et al.* History of the ribosome and the origin
> of translation. *Proc. Natl. Acad. Sci. U.S.A.* *112*, 15396–15401 (2015).
>
> 11.        Grosjean, H. & Westhof, E. An integrated, structure- and
> energy-based view of the genetic code. *Nucleic Acids Res.* *44*,
> 8020–8040 (2016).
>
> 12.        Root-Bernstein, M. & Root-Bernstein, R. The ribosome as a
> missing link in the evolution of life. *J. Theor. Biol.* *367*, 130–158
> (2015).
>
> 13.        Root-Bernstein, R. & Root-Bernstein, M. The ribosome as a
> missing link in prebiotic evolution II: Ribosomes encode ribosomal proteins
> that bind to common regions of their own mRNAs and rRNAs. *J Theor Biol*
> *397*, 115–127 (2016).
>
> 14.        Root-Bernstein, R. & Root-Bernstein, M. The Ribosome as a
> Missing Link in Prebiotic Evolution III: Over-Representation of tRNA- and
> rRNA-Like Sequences and Plieofunctionality of Ribosome-Related Molecules
> Argues for the Evolution of Primitive Genomes from Ribosomal RNA Modules. *Int
> J Mol Sci* *20*, (2019).
>
> 15.        Voorhees, R. M. & Ramakrishnan, V. Structural basis of the
> translational elongation cycle. *Annu. Rev. Biochem.* *82*, 203–236
> (2013).
>
> 16.        Ban, N., Nissen, P., Hansen, J., Moore, P. B. & Steitz, T. A.
> The complete atomic structure of the large ribosomal subunit at 2.4 A
> resolution. *Science* *289*, 905–920 (2000).
>
> 17.        Ben-Shem, A. *et al.* The structure of the eukaryotic ribosome
> at 3.0 Å resolution. *Science* *334*, 1524–1529 (2011).
>
> 18.        Wilson, D. N. & Doudna Cate, J. H. The structure and function
> of the eukaryotic ribosome. *Cold Spring Harb Perspect Biol* *4*, (2012).
>
> 19.        Wilson, D. N. & Nierhaus, K. H. Ribosomal proteins in the
> spotlight. *Crit. Rev. Biochem. Mol. Biol.* *40*, 243–267 (2005).
>
> 20.        Timsit, Y., Allemand, F., Chiaruttini, C. & Springer, M.
> Coexistence of two protein folding states in the crystal structure of
> ribosomal protein L20. *EMBO Rep.* *7*, 1013–1018 (2006).
>
> 21.        Selmer, M. *et al.* Structure of the 70S Ribosome Complexed
> with mRNA and tRNA. *Science* (2006) doi:10.1126/science.1131127.
>
> 22.        Timsit, Y., Acosta, Z., Allemand, F., Chiaruttini, C. &
> Springer, M. The role of disordered ribosomal protein extensions in the
> early steps of eubacterial 50 S ribosomal subunit assembly. *Int J Mol
> Sci* *10*, 817–834 (2009).
>
> 23.        Poirot, O. & Timsit, Y. Neuron-Like Networks Between Ribosomal
> Proteins Within the Ribosome. *Sci Rep* *6*, 26485 (2016).
>
> 24.        Timsit, Y. & Bennequin, D. Nervous-Like Circuits in the
> Ribosome Facts, Hypotheses and Perspectives. *Int J Mol Sci* *20*, (2019).
>
> 25.        Rhodin, M. H. J. & Dinman, J. D. An extensive network of
> information flow through the B1b/c intersubunit bridge of the yeast
> ribosome. *PLoS ONE* *6*, e20048 (2011).
>
> 26.        Meskauskas, A. & Dinman, J. D. A molecular clamp ensures
> allosteric coordination of peptidyltransfer and ligand binding to the
> ribosomal A-site. *Nucleic Acids Res.* *38*, 7800–7813 (2010).
>
> 27.        Sulima, S. O. *et al.* Eukaryotic rpL10 drives ribosomal
> rotation. *Nucleic Acids Res.* *42*, 2049–2063 (2014).
>
> 28.        Gulay, S. P. *et al.* Tracking fluctuation hotspots on the
> yeast ribosome through the elongation cycle. *Nucleic Acids Res.* *45*,
> 4958–4971 (2017).
>
> 29.        Rakauskaite, R. & Dinman, J. D. rRNA mutants in the yeast
> peptidyltransferase center reveal allosteric information networks and
> mechanisms of drug resistance. *Nucleic Acids Res.* *36*, 1497–1507
> (2008).
>
> 30.        Bowen, A. M. *et al.* Ribosomal protein uS19 mutants reveal
> its role in coordinating ribosome structure and function. *Translation
> (Austin)* *3*, e1117703 (2015).
>
> 31.        Kisly, I. *et al.* The Functional Role of eL19 and eB12
> Intersubunit Bridge in the Eukaryotic Ribosome. *J. Mol. Biol.* *428*,
> 2203–2216 (2016).
>
> 32.        Meskauskas, A., Russ, J. R. & Dinman, J. D. Structure/function
> analysis of yeast ribosomal protein L2. *Nucleic Acids Res.* *36*,
> 1826–1835 (2008).
>
> 33.        Zaher, H. S. & Green, R. Fidelity at the molecular level:
> lessons from protein synthesis. *Cell* *136*, 746–762 (2009).
>
> 34.        Wilson, D. N., Arenz, S. & Beckmann, R. Translation regulation
> via nascent polypeptide-mediated ribosome stalling. *Curr. Opin. Struct.
> Biol.* *37*, 123–133 (2016).
>
> 35.        Pechmann, S., Willmund, F. & Frydman, J. The ribosome as a hub
> for protein quality control. *Mol. Cell* *49*, 411–421 (2013).
>
> 36.        Juszkiewicz, S. *et al.* ZNF598 Is a Quality Control Sensor of
> Collided Ribosomes. *Mol Cell* *72*, 469-481.e7 (2018).
>
> 37.        Korostelev, A., Ermolenko, D. N. & Noller, H. F. Structural
> dynamics of the ribosome. *Curr Opin Chem Biol* *12*, 674–683 (2008).
>
> 38.        Paci, M. & Fox, G. E. Major centers of motion in the large
> ribosomal RNAs. *Nucleic Acids Res* *43*, 4640–4649 (2015).
>
> 39.        Paci, M. & Fox, G. E. Centers of motion associated with EF-Tu
> binding to the ribosome. *RNA Biol* *13*, 524–530 (2016).
>
> 40.        Genuth, N. R. & Barna, M. The Discovery of Ribosome
> Heterogeneity and Its Implications for Gene Regulation and Organismal Life. *Mol.
> Cell* *71*, 364–374 (2018).
>
> 41.        Dinman, J. D. Pathways to Specialized Ribosomes: The Brussels
> Lecture. *J. Mol. Biol.* *428*, 2186–2194 (2016).
>
> 42.        Timsit, Y., Sergeant-Perthuis, G. & Bennequin, D. Evolution of
> ribosomal protein network architectures. *Sci Rep* *11*, 625 (2021).
>
> 43.        Forterre, P. The universal tree of life: an update. *Front
> Microbiol* *6*, 717 (2015).
>
> 44.        Baluška, F. & Levin, M. On Having No Head: Cognition throughout
> Biological Systems. *Front Psychol* *7*, 902 (2016).
>
>
>
>
>
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>
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