Comparisons of the nucleotide substitution process among repetitive segments of the α- and β-spectrin genes

Journal of Molecular Evolution

Volumn 44, Issue 5, 1997, Pages 492-500

  Muse, Spencer V ^a,b   Clark, Andrew G ^a   Thomas, Graham H ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF MISSOURI   (United States)

Author keywords

Elliptocytosis; Gene duplication; Maximum likelihood; Spectrin; Spherocytosis; Substitution pattern; Substitution rate

Indexed keywords

DNA; FODRIN; NUCLEOTIDE; PROTEIN SUBUNIT; SPECTRIN;

ARTICLE; DNA SEQUENCE; GENE DUPLICATION; GENETIC HETEROGENEITY; HUMAN; MOLECULAR EVOLUTION; NONHUMAN; NUCLEIC ACID BASE SUBSTITUTION; STATISTICAL MODEL;

ANIMALS; BASE COMPOSITION; EVOLUTION, MOLECULAR; GENE CONVERSION; GENES; HUMANS; MODELS, GENETIC; PHYLOGENY; REPETITIVE SEQUENCES, NUCLEIC ACID; SPECTRIN;

EID: 0030915823     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006173     Document Type: Article

References (44)

1. Akaike H (1974) A new look at the statistical model identification. IEEE Trans Autom Contr 19:716-723
2. Arnheim N (1983) Concerted evolution of multigene families. In: Nei M, Koehn RK (eds) Evolution of genes and proteins. Sinauer. Sunderland, MA, pp 38-61
3. Becker P, Lux S (1995) Hereditary spherocytosis and hereditary elliptocytosis. In: Scriver C, Beaudet A, Sly W. Valle D (eds) The metabolic and molecular basis of inherited disease. McGraw Hill, New York, pp 3513-3560
4. Bennet V, Gilligan D (1993) The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol 9:27-66
5. Bloom M, Birkenmeier C, Barker J (1993) Complete nucleotide sequence of the murine erythroid β-spectrin cDNA and tissue-specific expression in normal and jaundiced mice. Blood 82:2906-2914
6. Byers T, Brandin E, Lue R, Winograd E, Branton D (1992) The complete sequence of drosophila beta-spectrin reveals supra-motifs containing eight 106-residue segments. Proc Natl Acad Sci USA 89:6187-6191
7. Coleman T, Fishkind D, Mooseker M, Morrow J (1989) Contributions of the β-subunit to spectrin structure and function. Cell Motil Cytoskeleton 12:248-263
8. Dhermy D (1991) The spectrin super-family. Biol Cell 71:249-254
9. Dubreuil R (1991) Structure and evolution of the actin crosslinking proteins. Bioessays 13:219-226
10. Dubreuil R, Byers T, Sillman A, Bar-Zvi D, Goldstein L, Branton D (1989) The complete sequence of drosophila alpha-spectrin: conservation of structural domains between alpha-spectrins and alpha-actinin. J Cell Biol 109:2197-2205
11. Felsenstein J (1981) Evolutionary trees from DNA sequences: a maximum likelihood approach. J Mol Evol 17:368-376
12. Hartwig J, Kwaitkowski D (1991) Actin-binding proteins. Curr Opin Cell Biol 3:87-97
13. Hasegawa M, Kishino H, Yano T (1985) Dating of the human-ape splitting by a molecular clock of mitochondrial DNA. J Mol Evol 22:160-174
14. Hemmings L, Kuhlamn P, Critchley D (1992) Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain. J Cell Biol 116:1369-1380
15. Hu R, Masayo W, Bennett V (1992) Characterization of human brain cDNA encoding the general isoform of β-spectrin. J Biol Chem 267:18715-18722
16. Hughes AL, Ota T, Nei M (1990) Positive Darwinian selection promotes charge profile diversity in the antigen-binding cleft of class I major-histocompatibility-complex molecules. Mol Biol Evol 7: 515-524
17. Jukes TH, Cantor CR (1969) Evolution of protein molecules. In: Munro HM (ed) Mammalian protein metabolism. Academic Press, New York, pp 21-132
18. Kumar S, Tamura K, Nei M (1993) MEGA: molecular evolutionary genetics analysis, version 1.01. The Pennsylvania State University, University Park, PA
19. Leto T, Fortugno-Erikson D, Barton D, Yang-Fang T, Francke U, Harris A, Morrow J, Marchesi V, Benz E Jr (1988) Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species. Mol Cell Biol 8:1-9
20. Li WH, Gojobori T (1983) Rapid evolution of goat and sheep globin genes following gene duplication. Mol Biol Evol 1:94-108
21. Li J, Nelson K, McWhorter AC, Whittam TS, Selander RK (1994) Recombinational basis of serovar diversity in Salmonella enterica. Proc Natl Acad Sci USA 91:2552-2556
22. Ma Y, Zimmer W, Riederer B, Goodman S (1993) The complete amino acid sequence for brain β spectrin (β fodrin): relationship to globin sequences. Mol Brain Res 18:87-99
23. Maynard Smith J (1992) Analyzing the mosaic structure of genes. J Mol Evol 34:126-129
24. McMahon A, Moon R (1987) Structure and evolution of a nonerythroid spectrin, human α-fodrin. Biol Soc Trans 15:804-807
25. Moon R, McMahon A (1990) Generation of diversity in nonerythroid spectrins. J Biol Chem 256:4427-4433
26. Muse SV, Gaut BS (1994) A likelihood approach for comparing synonymous and nonsynonymous nucleotide substitution rates with application to the chloroplast genome. Mol Biol Evol 11:715-724
27. Muse, SV, Gaut BS (1997) Comparing patterns of nucleotide substitution rates among chloroplast loci using the relative ratio test. Genetics (in press)
28. Rodriguez F, Oliver JF, Marin A, Medina JR (1990) The general stochastic model of nucleotide substitutions. J Theor Biol 142:485-501
29. Sahr K, Laurila P, Kotula L, Scarpa A, Coupai E, Linnenbach TLA, Winkelmann J, Speicher D, Marchesi V, Curtis P, Forget BG (1990) The complete cDNA and polypeptide sequences of human erythroid α-spectrin. J Biol Chem 265:4434-4443
30. Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425
31. Sawyer SA (1989) Statistical tests for detecting gene conversion. Mol Biol Evol 6:526-538
32. Speicher D, Marchesi V (1984) Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311:177-180
33. Speicher D, Welglarz L, DeSilva TM (1992) Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. J Biol Chem 267:14775-14782
34. Stephens JC (1985) Statistical methods of DNA sequence analysis: detection of intragenic recombination or gene conversion. Mol Biol Evol 2:539-556
35. Strickberger MW (1995) Evolution. Jones and Bartlett, Sudbury, MA
36. Tamura K, Nei M (1993) Estimation of the number of nucleotide substitutions in the control region of mitochondrial DNA in humans and chimpanzees. Mol Biol Evol 10:512-526
37. Tavaré S (1986) Some probabilistic and statistical problems in the analysis of DNA sequences. In: Miura RM (ed) Lectures on mathematics in the life sciences. Am Math Soc, Providence, RI, pp 57-86
38. Veil A, Branton D (1994) Interchain binding at the tail end of the drosophila spectrin molecule. Proc Natl Acad Sci USA 91:10839-10843
39. Veil A, Branton D (1996) Spectrin: on the path from structure to function. Curr Opin Cell Biol 8:49-55
40. Wasenius V, Saraste M, Salvén P, Erämaa M, Holm L, Lehto V (1989) Primary structure of the brain α-spectrin. J Cell Biol 108:79-93
41. Winkelman J, Chang J, Tse W, Marchesi V, Forget B (1990a) Full-length sequence of the cDNA for human erythroid β-spectrin. J Biol Chem 265:11827-11838
42. Winkelman J. Costa F, Linzie B, Forget B (1990b) β-spectrin in human skeletal muscle. J Biol Chem 265:20449-20454
43. Van Y, Winograd E, Veil A, Cronin T, Harrison S, Branton D (1993) Crystal structure of the repetitive segments of spectrin. Science 262:2027-2030
44. Zimmer EA, Martin SL, Beverley SM, Kan YK, Wilson AC (1980) Rapid duplication and loss of genes coding for the alpha chains of hemoglobin. Proc Natl Acad Sci USA 77:2158-2162