Evolution of Cytochrome C Investigated by the Maximum Parsimony Method

Overview

Journal J Mol Evol

Specialty Biochemistry

Date 1981 Jan 1

PMID 6267311

Citations 25

Authors

M L Baba

L L Darga

M Goodman

J Czelusniak

Affiliations

Soon will be listed here.

Abstract

Rates of evolution for cytochrome c over the past one billion years were calculated from a maximum parsimony dendrogram which approximates the phylogeny of 87 lineages. Two periods of evolutionary acceleration and deceleration apparently occurred for the cytochrome c molecule. The tempo of evolutionary change indicated by this analysis was compared to the patterns of acceleration and deceleration in the ancestry of several other proteins. The synchrony of these tempos of molecular change supports the notion that rapid genetic evolution accompanied periods of major adaptive radiations. Rates of change at different time in several structural-functional areas of cytochrome c were also investigated in order to test the Darwinian hypothesis that during periods of rapid evolution, functional sites accumulate proportionately more substitutions than areas with no known functions. Rates of change in four proposed functional groupings of sites were therefore compared to rates in areas of unknown function for several different time periods. This analysis revealed a significant increase in the rate of evolution for sites associated with the regions of cytochrome c oxidase and reductase interaction during the period between the emergence of the eutherian ancestor to the emergence of the anthropoid ancestor.

Citing Articles

Accelerated Evolution of Cytochrome in Higher Primates, and Regulation of the Reaction between Cytochrome and Cytochrome Oxidase by Phosphorylation.

Brand S, Scharlau M, Geren L, Hendrix M, Parson C, Elmendorf T Cells. 2022; 11(24).

PMID: 36552779 PMC: 9777161. DOI: 10.3390/cells11244014.

An Evolutionary Perspective on the Origin, Conservation and Binding Partner Acquisition of Tankyrases.

Sowa S, Bosetti C, Galera-Prat A, Johnson M, Lehtio L Biomolecules. 2022; 12(11).

PMID: 36421702 PMC: 9688111. DOI: 10.3390/biom12111688.

New Arabidopsis thaliana cytochrome c partners: a look into the elusive role of cytochrome c in programmed cell death in plants.

Martinez-Fabregas J, Diaz-Moreno I, Gonzalez-Arzola K, Janocha S, Navarro J, Hervas M Mol Cell Proteomics. 2013; 12(12):3666-76.

PMID: 24019145 PMC: 3861715. DOI: 10.1074/mcp.M113.030692.

Evolution of the couple cytochrome c and cytochrome c oxidase in primates.

Pierron D, Wildman D, Huttemann M, Letellier T, Grossman L Adv Exp Med Biol. 2012; 748:185-213.

PMID: 22729859 PMC: 3714796. DOI: 10.1007/978-1-4614-3573-0_8.

Silencing, positive selection and parallel evolution: busy history of primate cytochromes C.

Pierron D, Opazo J, Heiske M, Papper Z, Uddin M, Chand G PLoS One. 2011; 6(10):e26269.

PMID: 22028846 PMC: 3196546. DOI: 10.1371/journal.pone.0026269.

References

FITCH W, MARGOLIASH E . Construction of phylogenetic trees. Science. 1967; 155(3760):279-84. DOI: 10.1126/science.155.3760.279. View

Mandel N, Mandel G, Trus B, Rosenberg J, Carlson G, DICKERSON R . Tuna cytochrome c at 2.0 A resolution. III. Coordinate optimization and comparison of structures. J Biol Chem. 1977; 252(13):4619-36. View

Moore G, BARNABAS J, Goodman M . A method for constructing maximum parsimony ancestral amino acid sequences on a given network. J Theor Biol. 1973; 38(3):459-85. DOI: 10.1016/0022-5193(73)90252-x. View

Goodman M, PECHERE J, Haiech J, Demaille J . Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins. J Mol Evol. 1979; 13(4):331-52. DOI: 10.1007/BF01731373. View

Osheroff N, Borden D, Koppenol W, MARGOLIASH E . Electrostatic interactions in cytochrome c. The role of interactions between residues 13 and 90 and residues 79 and 47 in stabilizing the heme crevice structure. J Biol Chem. 1980; 255(4):1689-97. View

DICKERSON R . The structure and history of an ancient protein. Sci Am. 1972; 226(4):58-70 passim. DOI: 10.1038/scientificamerican0472-58. View

Ng S, Smith M, Smith H, Millett F . Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. Biochemistry. 1977; 16(23):4975-8. DOI: 10.1021/bi00642a006. View

Shaw D, Williams K, Smith E, Birt L . The amino acid sequence of cytochrome c from the blowfly Lucilia cuprina. Biochim Biophys Acta. 1978; 532(1):179-84. DOI: 10.1016/0005-2795(78)90461-0. View

Smith L, Davies H, Nava M . Oxidation and reduction of soluble cytochrome c by membrane-bound oxidase and reductase systems. J Biol Chem. 1974; 249(9):2904-10. View

10.

MARGOLIASH E . PRIMARY STRUCTURE AND EVOLUTION OF CYTOCHROME C. Proc Natl Acad Sci U S A. 1963; 50:672-9. PMC: 221244. DOI: 10.1073/pnas.50.4.672. View

11.

MARGOLIASH E, SCHEJTER A . Cytochrome c. Adv Protein Chem. 1966; 21:113-286. DOI: 10.1016/s0065-3233(08)60128-x. View

12.

DICKERSON R, Timkovich R, Almassy R . The cytochrome fold and the evolution of bacterial energy metabolism. J Mol Biol. 1976; 100(4):473-91. DOI: 10.1016/s0022-2836(76)80041-1. View

13.

Moore G, Goodman M, Callahan C, Holmquist R, Moise H . Stochastic versus augmented maximum parsimony method for estimating superimposed mutations in the divergent evolution of protein sequences. Methods tested on cytochrome c amino acid sequences. J Mol Biol. 1976; 105(1):15-37. DOI: 10.1016/0022-2836(76)90193-5. View

14.

Kang C, Brautigan D, Osheroff N, MARGOLIASH E . Definitaion of cytochrome c binding domains by chemical modification. Reaction of carboxydinitrophenyl- and trinitrophenyl-cytochromes c with baker's yeast cytochrome c peroxidase. J Biol Chem. 1978; 253(18):6502-10. View

15.

Moore G . Proof of the populous path algorithm for missing mutations in parsimony trees. J Theor Biol. 1977; 66(1):95-106. DOI: 10.1016/0022-5193(77)90314-9. View

16.

Thompson R, Borden D, Tarr G, MARGOLIASH E . Heterogeneity of amino acid sequence in hippopotamus cytochrome c. J Biol Chem. 1978; 253(24):8957-61. View

17.

Jemmerson R, MARGOLIASH E . Topographic antigenic determinants on cytochrome c. Immunoadsorbent separation of the rabbit antibody populations directed against horse cytochrome. J Biol Chem. 1979; 254(24):12706-16. View

18.

MARGOLIASH E, FITCH W, DICKERSON R . Molecular expression of evolutinary phenomena in the primary and tertiary structures of cytochrome c. Brookhaven Symp Biol. 1968; 21(2):259-305. View

19.

Jemmerson R, MARGOLIASH E . Specificity of the antibody response of rabbits to a self-antigen. Nature. 1979; 282(5738):468-71. DOI: 10.1038/282468a0. View

20.

Brautigan D, Ferguson-Miller S, Tarr G, MARGOLIASH E . Definition of cytochrome c binding domains by chemical modification. II. Identification and properties of singly substituted carboxydinitrophenyl cytochromes c at lysines 8, 13, 22, 27, 39, 60, 72, 87, and 99. J Biol Chem. 1978; 253(1):140-8. View