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The RNA dreamtime: modern cells feature proteins that might have supported a prebiotic polypeptide world but nothing indicates that RNA world ever was.

Kurland, Charles LU (2010) In BioEssays 32(10). p.866-871
Abstract
Modern cells present no signs of a putative prebiotic RNA world. However, RNA coding is not a sine qua non for the accumulation of catalytic polypeptides. Thus, cellular proteins spontaneously fold into active structures that are resistant to proteolysis. The law of mass action suggests that binding domains are stabilized by specific interactions with their substrates. Random polypeptide synthesis in a prebiotic world has the potential to initially produce only a very small fraction of polypeptides that can fold spontaneously into catalytic domains. However, that fraction can be enriched by proteolytic activities that destroy the unfolded polypeptides and regenerate amino acids that can be recycled into polypeptides. In this open system... (More)
Modern cells present no signs of a putative prebiotic RNA world. However, RNA coding is not a sine qua non for the accumulation of catalytic polypeptides. Thus, cellular proteins spontaneously fold into active structures that are resistant to proteolysis. The law of mass action suggests that binding domains are stabilized by specific interactions with their substrates. Random polypeptide synthesis in a prebiotic world has the potential to initially produce only a very small fraction of polypeptides that can fold spontaneously into catalytic domains. However, that fraction can be enriched by proteolytic activities that destroy the unfolded polypeptides and regenerate amino acids that can be recycled into polypeptides. In this open system scenario the stable domains that accumulate and the chemical environment in which they are accumulated are linked through self coding of polypeptide structure. Such open polypeptide systems may have been the precursors to the cellular ribonucleoprotein (RNP) world that evolved subsequently. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
non-ribosomal peptidyl transferase, domain selection, polypeptides, proteolysis, ribozymes
in
BioEssays
volume
32
issue
10
pages
866 - 871
publisher
John Wiley & Sons
external identifiers
  • wos:000283103900006
  • scopus:77957193832
ISSN
0265-9247
DOI
10.1002/bies.201000058
language
English
LU publication?
yes
id
17c69a39-e406-4aca-94f1-b4afa23601e4 (old id 1688697)
date added to LUP
2010-10-21 16:28:09
date last changed
2018-07-01 03:23:15
@article{17c69a39-e406-4aca-94f1-b4afa23601e4,
  abstract     = {Modern cells present no signs of a putative prebiotic RNA world. However, RNA coding is not a sine qua non for the accumulation of catalytic polypeptides. Thus, cellular proteins spontaneously fold into active structures that are resistant to proteolysis. The law of mass action suggests that binding domains are stabilized by specific interactions with their substrates. Random polypeptide synthesis in a prebiotic world has the potential to initially produce only a very small fraction of polypeptides that can fold spontaneously into catalytic domains. However, that fraction can be enriched by proteolytic activities that destroy the unfolded polypeptides and regenerate amino acids that can be recycled into polypeptides. In this open system scenario the stable domains that accumulate and the chemical environment in which they are accumulated are linked through self coding of polypeptide structure. Such open polypeptide systems may have been the precursors to the cellular ribonucleoprotein (RNP) world that evolved subsequently.},
  author       = {Kurland, Charles},
  issn         = {0265-9247},
  keyword      = {non-ribosomal peptidyl transferase,domain selection,polypeptides,proteolysis,ribozymes},
  language     = {eng},
  number       = {10},
  pages        = {866--871},
  publisher    = {John Wiley & Sons},
  series       = {BioEssays},
  title        = {The RNA dreamtime: modern cells feature proteins that might have supported a prebiotic polypeptide world but nothing indicates that RNA world ever was.},
  url          = {http://dx.doi.org/10.1002/bies.201000058},
  volume       = {32},
  year         = {2010},
}