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29 March 2024 |
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The first peptides: the evolutionary transition between prebiotic amino acids and early proteins | Peter van der Gulik
; Serge Massar
; Dimitri Gilis
; Harry Buhrman
; Marianne Rooman
; | Date: |
15 Sep 2009 | Abstract: | The issues we attempt to tackle here are what the first peptides did look
like when they emerged on the primitive earth, and what simple catalytic
activities they fulfilled. We conjecture that the early functional peptides
were short (3 to 8 amino acids long), were made of those amino acids, Gly, Ala,
Val and Asp, that are abundantly produced in many prebiotic synthesis
experiments and observed in meteorites, and that the neutralization of Asp’s
negative charge is achieved by metal ions. We further assume that some traces
of these prebiotic peptides still exist, in the form of active sites in
present-day proteins. Searching these proteins for prebiotic peptide candidates
led us to identify three main classes of motifs, bound mainly to Mg^{2+} ions:
D(F/Y)DGD corresponding to the active site in RNA polymerases, DGD(G/A)D
present in some kinds of mutases, and DAKVGDGD in dihydroxyacetone kinase. All
three motifs contain a DGD submotif, which is suggested to be the common
ancestor of all active peptides. Moreover, all three manipulate phosphate
groups, which was probably a very important biological function in the very
first stages of life. The statistical significance of our results is supported
by the frequency of these motifs in today’s proteins, which is three times
higher than expected by chance, with a P-value of 3 10^{-2}. The implications
of our findings in the context of the appearance of life and the possibility of
an experimental validation are discussed. | Source: | arXiv, 0909.2832 | Services: | Forum | Review | PDF | Favorites |
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