Molecular Evolution of Myoglobin and the Fossil Record: a Phylogenetic Synthesis

Romero‐Herrera, A. E.; Lehmann, H.; Joysey, K. A.; Friday, Adrian

doi:10.1038/246389a0

Cited by 150 publications

(38 citation statements)

References 71 publications

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“…The major structural proteins of the M7, RD-114, R-MuLV, and SSAV type C viruses were purified to apparent homogeneity (3), and 10-,Og samples were iodinated (23) to specific activities of [5][6][7][8][9][10] uCi/Mug. Competitive radioimmunoassays (24,25,3) and determination of radioactivity (3) were as described.…”

Section: Methodsmentioning

confidence: 99%

“…Hybrids formed between [3H]DNA transcripts of baboon type C viral RNA and Old World monkey cellular DNA show a greater degree of base pair mismatching than do hybrids obtained with baboon cellular DNA, indicating that the endogenous virogenes in these related species have evolved away from one another (5,6) during the 15 million years since the species diverged (7).…”

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confidence: 99%

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Type C Viral Expression in Primate Tissues

Sherr¹,

Benveniste²,

Todaro³

1974

Proc. Natl. Acad. Sci. U.S.A.

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Nucleic acid sequences homologous to a 13HJDNA transcript prepared from an endogenous baboon type C virus are readily detected in both the cellular DNA and RNA of several different Old World monkeys. Competitive radioimmunoassays for the major viral protein (p30) of baboon type C viruses detect viral antigen in a normal stumptail spleen and a rhesus ovarian carcinoma.The p30 antigen from these tissues is closely related by several immunologic criteria to the p30 protein of baboon type C viruses. The results indicate that normal primate tissues transcribe endogenous viral-specific RNA and translate at least one viral structural protein.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Type C Viral Expression in Primate Tissues

Sherr¹,

Benveniste²,

Todaro³

1974

Proc. Natl. Acad. Sci. U.S.A.

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“…Also many workers have demonstrated that different lineages mutate at varying rates (Goodman et at. 1971;Dayhoff 1972;Romero-Herrera et al 1973;Goodman et al 1975), suggesting that the assumption of a constant rate of mutation, necessary for divergence point estimations, may not be valid.…”

Section: Discussionmentioning

confidence: 99%

Studies on Monotreme Proteins. VI. Amino Acid Sequence of the ß-Chain of Haemoglobin From the Platypus, Ornithorhynchus anatinus

Whittaker¹,

Thompson²

1975

Aust. Jnl. Of Bio. Sci.

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The amino acid sequence of the 146 residues of the p-chain of the major haemoglobin from the platypus has been determined. The soluble peptides derived from the chain by tryptic digestion were isolated by paper ionophoresis and chromatography. The amino acid sequences were determined by the dansyl-Edman procedure or by further digestion with other enzymes. The tryptic peptides were aligned by homology with other p-globins. There were 14 changes in sequence compared with echidna p-chain.The number of changes in sequence compared with human p-chain is 34 which is less than the 39 changes between human and platypus oc-chains. Generally there are more changes between p-chains; there are only three other examples reported where there are more changes between oc-chains than p-chains, these are of echidna, rabbit and dog globins.By comparison with the 'contact sites' in horse haemoglobin there is one change in p-haem contacts, three changes in Pr-OCl contacts and no changes in Pr-(1.1 contacts.The date of divergence of the monotremes from the other mammals was estimated at 132 ± 33 million years, based on the number of amino acid differences between species and allowing for multiple mutations during the evolutionary period. This estimate differs widely from the estimate given by similar treatment of the oc-chain sequences and the significance of this discrepancy to the validity of the method is discussed.

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“…The phylogenetic tree derived from palaeontological evidence was altered to accommodate, where possible, the dates suggested by Romero-Herrera et al (1973). The older alternative for the marsupial-placental divergence was used.…”

Section: Isolation Of Tryptic Pep Tidesmentioning

confidence: 99%

Studies on Monotreme Proteins. V. Amino Acid Sequence of the a-Chain of Haemoglobin From the Platypus, Ornithorhynchus anatinus

Whittaker¹,

Eo²

1974

Aust. Jnl. Of Bio. Sci.

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Blood from the platypus contained three haemoglobins which were separated by chromatography on DEAE-Sephadex. The major component, Hb-I, was converted to globin and fractionated into the oc-and p-chains by chromatography on eM-cellulose in 8M urea-thiol buffers, and the complete amino acid sequence of the 141 residues of the oc-chain were determined. Peptides derived from the oc-chain by tryptic digestion were isolated by paper ionophoresis and chromatography. The amino acid sequences were determined by the dansyl-Edman procedure or by further digestion with other enzymes.The amino acid sequence showed 16 changes from the oc-globin of the other extant monotreme, the echidna. There were 39 changes from the human oc-globin sequence. By comparison with the 'contact sites' in horse haemoglobin there is one change in the oc-haem contacts, four changes in the OCI-PI contacts and no changes in the OC,-P2 contacts.The date of divergence of the monotremes from the other mammals was estimated to be 180± 37 million years, based on the number of amino acid differences between species and allowing for multiple mutations during the evolutionary period. The significance of this estimate in relation to the time of divergence of marsupials is discussed.

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Molecular Evolution of Myoglobin and the Fossil Record: a Phylogenetic Synthesis

Cited by 150 publications

References 71 publications

Type C Viral Expression in Primate Tissues

Type C Viral Expression in Primate Tissues

Studies on Monotreme Proteins. VI. Amino Acid Sequence of the ß-Chain of Haemoglobin From the Platypus, Ornithorhynchus anatinus

Studies on Monotreme Proteins. V. Amino Acid Sequence of the a-Chain of Haemoglobin From the Platypus, Ornithorhynchus anatinus

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