Reconstructing the evolutionary history of the artiodactyl ribonuclease superfamily

  title={Reconstructing the evolutionary history of the artiodactyl ribonuclease superfamily},
  author={Thomas M. Jermann and Jochen G. Opitz and Joseph Stackhouse and Steven A. Benner},
THE sequences of proteins from ancient organisms can be reconstructed from the sequences of their descendants by a procedure that assumes that the descendant proteins arose from the extinct ancestor by the smallest number of independent evolutionary events (‘parsimony’)1,2. The reconstructed sequences can then be prepared in the laboratory and studied3,4. Thirteen ancient ribonucleases (RNases) have been reconstructed as intermediates in the evolution of the RNase protein family in artiodactyls… 

Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins

This study resurrects candidate sequences for elongation factors of the Tu family found at ancient nodes in the bacterial evolutionary tree, and measures their activities as a function of temperature to suggest that the ancient bacteria that hosted these particular genes were thermophiles, and neither hyperthermophiles nor mesophiles.

An ancient evolutionary connection between Ribonuclease A and EndoU families

It is shown that bacterial and homologous archaeal polymorphic toxin ribonucleases with a known or predicted ribonuclease A-like fold are distant homologs of the ribon nucleases from the EndoU family, found in all domains of cellular life and in viruses.

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Using actual genomic sequences from 19 extant mammals, 1.1 Mb of ancient genome sequence around the CFTR locus is reconstructed and detailed examination suggests the reconstruction is accurate and that it allows us to identify features in modern species, such as remnants of ancient transposon insertions that were not identified by direct analysis.

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The fossil record, and genome sequences derived from it, has the potential to elucidate ancient, extinct forms of life, acting as missing links to fill evolution‐ ary gaps; however, the sequenced fossil genome is very limited, mainly due to the condition of samples and the challenges of preparing them.

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The primary challenge of ASR remains in accurately inferring ancestral states, despite the uncertainty arising from evolutionary models, incomplete sequences and limited phylogenetic trees, and an escalation in the number of ancient proteins resurrected in the last decade is highlighted.



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Amino acid sequences of 39 mammalian ribonucleases have been used to construct trees by the maximum parsimony procedure and no definite conclusions can be drawn about the order of divergence of the perissodactyls, the rodents, and the group consisting of artiodactylS plus cetaceans.

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Toward Defining the Course of Evolution: Minimum Change for a Specific Tree Topology

A method is presented that is asserted to provide all hypothetical ancestral character states that are consistent with describing the descent of the present-day character states in a minimum number of changes of state using a predetermined phylogenetic relationship among the taxa represented.

Expression of bovine pancreatic ribonuclease A in Escherichia coli.

The procedure here makes RNase A available for the first time as a model for studying structure-function relationships in proteins using site-directed mutagenesis, even when applied to particularly complicated expression problem.

Primary structure of a ribonuclease from bovine brain.

The primary structure of a pyrimidine base-specific ribonuclease from bovine brain was determined and it consists of 140 amino acid residues, and it is 16 amino acids residues longer than RNase A at the carboxyl-terminal.

Use of a trypsin-pulse method to study the refolding pathway of ribonuclease.

The results suggest that the 31 - 39 region of the ribonuclease chain is not important for early steps which direct the pathway of refolding, which suggests that this part of the sequence is still accessible at early stages ofRefolding, when a hydrogen-bonded network is formed.

Comparative base specificity, stability, and lectin activity of two lectins from eggs of Rana catesbeiana and R. japonica and liver ribonuclease from R. catesbeiana.

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