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M O Dayhoff

Publications and source records attributed to M O Dayhoff.

At least 19 recordsLinked to original sources
PubMed1982

Evolution of major metabolic innovations in the precambrian.

A combination of the information on the metabolic capabilities of prokaryotes with a composite phylogenetic tree depicting an overview of prokaryote evolution based on the sequences of bacterial ferredoxin, 2Fe-2S ferredoxin, 5S ribosomal RNA, and c-type cytochromes shows three zones of major metabolic innovation in the Precambrian. The middle of these, which reflects the genesis of oxygen-releasing photosynthesis and aerobic respiration, links metabolic innovations of the anaerobic stem on the one hand and, on the other, proliferation of aerobic bacteria and the symbiotic associations leading to the eukaryotes. We consider especially those pathways where information on the structure of the enzymes is known. Halobacterium and Thermoplasma (archaebacteria) do not belong to a totally independent line on the basis of the composite tree but branch from the eukaryote cytoplasmic line.

Bacteria↗
PubMed1982

Viral src gene products are related to the catalytic chain of mammalian cAMP-dependent protein kinase.

The transforming protein sequences translated from the Rous avian and Moloney murine sarcoma virus src genes are shown to be related to the catalytic chain of bovine cAMP-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37). The avian transforming protein, also a protein kinase, shows greatest homology with the bovine protein kinase in the carboxyl-terminal half, where the protein kinase activity is localized. Moreover, lysine occurs in the inferred transforming protein sequences at the position homologous with the proposed ATP-binding lysine of the bovine protein kinase. This relationship is consistent with the hypothesis that the src genes originated in the host genomes, in which they are members of a superfamily of distantly related protein kinases that are normal constituents of mammalian cells. In the host, these sequences are much more highly conserved than in the viruses.

Amino Acid Sequence↗
PubMed1981

Data bank.

Explore the source record for details and available documents.

Base Sequence↗
PubMed1980

Nucleic acid sequence bank.

In the report by T. Kakunaga and J. D. Crow (25 July, p. 505), Fig. 1 on page 506 should have been printed as follows: [See figure in the PDF file]

Base Sequence↗
PubMed1980

Origins of immunoglobulin heavy chain domains.

Using computer programs that analyze the evolutionary history and probability of relationship of protein sequences, we have investigated the gene duplication events that led to the present configuration of immunoglobulin C regions, with particular attention to the origins of the homology regions (domains) of the heavy chains. We conclude that all of the sequenced heavy chains share a common ancestor consisting of four domains and that the two shorter heavy chains, alpha and gamma, have independently lost most of the second domain. These conclusions allow us to align corresponding regions of these sequences for the purpose of deriving evolutionary trees. Three independent internal gene duplications are postulated to explain the observed pattern of relationships among the four domains: first a duplication of the ancestral single domain C region, followed by independent duplications of the resulting first and last domains. In these studies there was no evidence of crossing-over and recombination between ancestral chains of different classes; however, certain types of recombinations would not be detectable from the available sequence data.

Biological Evolution↗