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Volumn 74, Issue 2, 2008, Pages 199-207

Compensatory evolution in diploid populations

Author keywords

Compensatory evolution; Compensatory neutral mutation model; Heterodimer; Molecular evolution; Population genetics

Indexed keywords

EVOLUTION; MUTATION; POPULATION GENETICS;

EID: 49749146717     PISSN: 00405809     EISSN: 10960325     Source Type: Journal    
DOI: 10.1016/j.tpb.2008.07.002     Document Type: Article
Times cited : (5)

References (48)
  • 2
    • 1642346218 scopus 로고    scopus 로고
    • Pleiotropic effect of disrupting a conserved sequence involved in a long-range compensatory interaction in the Drosophila Adh
    • Baines J.F., Parsch J., and Stephan W. Pleiotropic effect of disrupting a conserved sequence involved in a long-range compensatory interaction in the Drosophila Adh. Gene. Genetics 166 (2004) 237-242
    • (2004) Gene. Genetics , vol.166 , pp. 237-242
    • Baines, J.F.1    Parsch, J.2    Stephan, W.3
  • 3
    • 0037772382 scopus 로고    scopus 로고
    • Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase
    • Bauer P.M., Fulton D., Boo Y.C., Sorescu G.P., Kemp B.E., Jo H., and Sessa W.C. Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase. J. Biol. Chem. 278 (2003) 14841-14849
    • (2003) J. Biol. Chem. , vol.278 , pp. 14841-14849
    • Bauer, P.M.1    Fulton, D.2    Boo, Y.C.3    Sorescu, G.P.4    Kemp, B.E.5    Jo, H.6    Sessa, W.C.7
  • 5
    • 0141593581 scopus 로고    scopus 로고
    • Compensatory evolution of a precursor messenger RNA secondary structure in the Drosophila melanogaster Adh gene
    • Chen Y., and Stephan W. Compensatory evolution of a precursor messenger RNA secondary structure in the Drosophila melanogaster Adh gene. Proc. Natl. Acad. Sci. USA 100 (2003) 11499-11504
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11499-11504
    • Chen, Y.1    Stephan, W.2
  • 6
    • 40549121635 scopus 로고    scopus 로고
    • Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer
    • Clapier C.R., Chakravarthy S., Petosa C., Fernández-Tornero C., Luger K., and Müller C.W. Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. Proteins 71 (2008) 1-7
    • (2008) Proteins , vol.71 , pp. 1-7
    • Clapier, C.R.1    Chakravarthy, S.2    Petosa, C.3    Fernández-Tornero, C.4    Luger, K.5    Müller, C.W.6
  • 7
    • 0037452557 scopus 로고    scopus 로고
    • Protein-protein interactions between Cytochrome b and the Fe-S protein subunits during QH(2) oxidation and large-scale domain movement in the bc(1)
    • Darrouzet E., and Daldal F. Protein-protein interactions between Cytochrome b and the Fe-S protein subunits during QH(2) oxidation and large-scale domain movement in the bc(1). Complex. Biochemistry 42 (2003) 1499-1507
    • (2003) Complex. Biochemistry , vol.42 , pp. 1499-1507
    • Darrouzet, E.1    Daldal, F.2
  • 8
    • 10044231838 scopus 로고    scopus 로고
    • Electrostatic repulsion, compensatory mutations, and long-range non-additive effects at the dimerization interface of the HIV capsid protein
    • del Alamo N., and Mateu M.G. Electrostatic repulsion, compensatory mutations, and long-range non-additive effects at the dimerization interface of the HIV capsid protein. J. Mol. Biol. 345 (2005) 893-906
    • (2005) J. Mol. Biol. , vol.345 , pp. 893-906
    • del Alamo, N.1    Mateu, M.G.2
  • 9
    • 0036277312 scopus 로고    scopus 로고
    • Roles of diversifying selection and coordinated evolution in the evolution of amphibian antimicrobial peptides
    • Duda Jr. T.F., Vanhoye D., and Nicolas P. Roles of diversifying selection and coordinated evolution in the evolution of amphibian antimicrobial peptides. Mol. Biol. Evol. 19 (2002) 858-864
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 858-864
    • Duda Jr., T.F.1    Vanhoye, D.2    Nicolas, P.3
  • 10
    • 10344231169 scopus 로고
    • A limit theorem for two locus diffusion models in population genetics
    • Ethier S.N. A limit theorem for two locus diffusion models in population genetics. J. Appl. Probab. 16 (1979) 402-408
    • (1979) J. Appl. Probab. , vol.16 , pp. 402-408
    • Ethier, S.N.1
  • 11
    • 0012945288 scopus 로고
    • Limit theorems for absorption times of genetic models
    • Ethier S.N. Limit theorems for absorption times of genetic models. Ann. Probab. 7 (1979) 622-638
    • (1979) Ann. Probab. , vol.7 , pp. 622-638
    • Ethier, S.N.1
  • 13
    • 0037442510 scopus 로고    scopus 로고
    • Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization
    • Fleck M.W., Cornell E., and Mah S.J. Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization. J. Neurosci. 23 (2003) 1219-1227
    • (2003) J. Neurosci. , vol.23 , pp. 1219-1227
    • Fleck, M.W.1    Cornell, E.2    Mah, S.J.3
  • 14
    • 0025678383 scopus 로고
    • Molecular clock of viral evolution, and the neutral theory
    • Gojobori T., Moriyama E.N., and Kimura M. Molecular clock of viral evolution, and the neutral theory. Proc. Natl. Acad. Sci. USA 87 (1990) 10015-10018
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 10015-10018
    • Gojobori, T.1    Moriyama, E.N.2    Kimura, M.3
  • 15
    • 33646544356 scopus 로고    scopus 로고
    • Signaling interactions between the aerotaxis transducer Aer and heterologous chemoreceptors in Escherichia coli
    • Gosink K.K., Burón-Barral M.D.C., and Parkinson J.S. Signaling interactions between the aerotaxis transducer Aer and heterologous chemoreceptors in Escherichia coli. J. Bacteriol. 188 (2006) 3487-3493
    • (2006) J. Bacteriol. , vol.188 , pp. 3487-3493
    • Gosink, K.K.1    Burón-Barral, M.D.C.2    Parkinson, J.S.3
  • 17
    • 33646766064 scopus 로고    scopus 로고
    • Correlated mutations: Advances and limitations. A study on fusion proteins and on the Cohesin-Docker in families
    • Halperin I., Wolfson H., and Nussinov R. Correlated mutations: Advances and limitations. A study on fusion proteins and on the Cohesin-Docker in families. Proteins Structure Function Bioinform. 63 (2006) 832-845
    • (2006) Proteins Structure Function Bioinform. , vol.63 , pp. 832-845
    • Halperin, I.1    Wolfson, H.2    Nussinov, R.3
  • 18
    • 4243559860 scopus 로고    scopus 로고
    • Compensatory neutral mutations on the evolution of RNA
    • Higgs P.G. Compensatory neutral mutations on the evolution of RNA. Genetica 102-103 (1998) 91-101
    • (1998) Genetica , vol.102-103 , pp. 91-101
    • Higgs, P.G.1
  • 19
    • 0029805846 scopus 로고    scopus 로고
    • Average time until fixation of mutants with compensatory fitness interaction
    • Iizuka M., and Takefu M. Average time until fixation of mutants with compensatory fitness interaction. Genes Genetic Syst. 71 (1996) 167-173
    • (1996) Genes Genetic Syst. , vol.71 , pp. 167-173
    • Iizuka, M.1    Takefu, M.2
  • 20
    • 0034805377 scopus 로고    scopus 로고
    • Selection intensity against deleterious mutations in RNA secondary structures and rate of compensatory nucleotide substitutions
    • Innan H., and Stephan W. Selection intensity against deleterious mutations in RNA secondary structures and rate of compensatory nucleotide substitutions. Genetics 159 (2001) 389-399
    • (2001) Genetics , vol.159 , pp. 389-399
    • Innan, H.1    Stephan, W.2
  • 21
    • 41149150650 scopus 로고    scopus 로고
    • Co-evolution and co-adaptation in protein networks
    • Juan D., Pazos F., and Valencia A. Co-evolution and co-adaptation in protein networks. FEBS Lett. 582 (2008) 1225-1230
    • (2008) FEBS Lett. , vol.582 , pp. 1225-1230
    • Juan, D.1    Pazos, F.2    Valencia, A.3
  • 22
    • 0033035418 scopus 로고    scopus 로고
    • Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity
    • Kiernan R.E., Ono A., and Freed E.O. Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity. J. Virol. 73 (1999) 4728-4737
    • (1999) J. Virol. , vol.73 , pp. 4728-4737
    • Kiernan, R.E.1    Ono, A.2    Freed, E.O.3
  • 23
    • 52449148668 scopus 로고
    • The role of compensatory neutral mutations in molecular evolution
    • Kimura M. The role of compensatory neutral mutations in molecular evolution. J. Genetics 64 (1985) 7-19
    • (1985) J. Genetics , vol.64 , pp. 7-19
    • Kimura, M.1
  • 24
    • 0041324003 scopus 로고
    • Diffusion models in population genetics with special reference to fixation time of molecular mutants under mutational pressure
    • Ohta T., and Aoki K. (Eds), Japan Sci. Soc. Press, Tokyo Springer-Verlag, Berlin
    • Kimura M. Diffusion models in population genetics with special reference to fixation time of molecular mutants under mutational pressure. In: Ohta T., and Aoki K. (Eds). Population Genetics and Molecular Evolution (1985), Japan Sci. Soc. Press, Tokyo 19-39 Springer-Verlag, Berlin
    • (1985) Population Genetics and Molecular Evolution , pp. 19-39
    • Kimura, M.1
  • 25
    • 0029026878 scopus 로고
    • Maintenance of pre-mRNA secondary structure by epistatic selection
    • Kirby D.A., Muse S.V., and Stephan W. Maintenance of pre-mRNA secondary structure by epistatic selection. Proc. Natl. Acad. Sci. USA 92 (1995) 9047-9051
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9047-9051
    • Kirby, D.A.1    Muse, S.V.2    Stephan, W.3
  • 27
    • 9444269272 scopus 로고    scopus 로고
    • Compensated deleterious mutations in insect genomes
    • Kulathinal R.J., Bettencourt B.R., and Hartl D.L. Compensated deleterious mutations in insect genomes. Science 306 (2004) 1553-1554
    • (2004) Science , vol.306 , pp. 1553-1554
    • Kulathinal, R.J.1    Bettencourt, B.R.2    Hartl, D.L.3
  • 28
    • 0034725998 scopus 로고    scopus 로고
    • Identification of a second site compensatory mutation in the Fe-protein that allows diazotrophic growth of Azotobacter vinelandii UW97
    • Lei S., Pulakat L., Suh M., and Gavini N. Identification of a second site compensatory mutation in the Fe-protein that allows diazotrophic growth of Azotobacter vinelandii UW97. FEBS Lett. 478 (2000) 192-196
    • (2000) FEBS Lett. , vol.478 , pp. 192-196
    • Lei, S.1    Pulakat, L.2    Suh, M.3    Gavini, N.4
  • 29
    • 49749115244 scopus 로고    scopus 로고
    • Littler, R.A., 1976. The independent loci model as a limit of a two locus model. Research Report No. 41. University of Waikato, Dept. of Math
    • Littler, R.A., 1976. The independent loci model as a limit of a two locus model. Research Report No. 41. University of Waikato, Dept. of Math
  • 30
    • 0018029874 scopus 로고
    • Fixation times and probabilities for an independent loci model in genetics
    • Littler R.A., and Good A.J. Fixation times and probabilities for an independent loci model in genetics. Theoret. Popul. Biol. 14 (1978) 204-214
    • (1978) Theoret. Popul. Biol. , vol.14 , pp. 204-214
    • Littler, R.A.1    Good, A.J.2
  • 31
    • 0032584233 scopus 로고    scopus 로고
    • Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization
    • MacKenzie K.R., and Engelman D.M. Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization. Proc. Natl. Acad. Sci. USA 95 (1998) 3583-3590
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3583-3590
    • MacKenzie, K.R.1    Engelman, D.M.2
  • 32
    • 0036431723 scopus 로고    scopus 로고
    • Compensatory adaptation to the deleterious effect of antibiotic resistance in Salmonella typhimurium
    • Maisnier-Patin S., Berg O.G., Liljas L., and Andersson D.I. Compensatory adaptation to the deleterious effect of antibiotic resistance in Salmonella typhimurium. Mol. Microbiol. 46 (2002) 355-366
    • (2002) Mol. Microbiol. , vol.46 , pp. 355-366
    • Maisnier-Patin, S.1    Berg, O.G.2    Liljas, L.3    Andersson, D.I.4
  • 33
    • 0033616825 scopus 로고    scopus 로고
    • Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization
    • Mateu M.G., and Fersht A.R. Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization. Proc. Natl. Acad. Sci. USA 96 (1999) 3595-3599
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3595-3599
    • Mateu, M.G.1    Fersht, A.R.2
  • 34
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • McCoy A.J., Epa V.C., and Colman P.M. Electrostatic complementarity at protein/protein interfaces. J. Mol. Biol. 268 (1997) 570-584
    • (1997) J. Mol. Biol. , vol.268 , pp. 570-584
    • McCoy, A.J.1    Epa, V.C.2    Colman, P.M.3
  • 35
    • 1642363503 scopus 로고    scopus 로고
    • Compensatory evolution in the human malaria parasite Plasmodium ovale
    • McCutchan T.F., Rathore D., and Li J. Compensatory evolution in the human malaria parasite Plasmodium ovale. Genetics 166 (2004) 637-640
    • (2004) Genetics , vol.166 , pp. 637-640
    • McCutchan, T.F.1    Rathore, D.2    Li, J.3
  • 36
    • 0030013435 scopus 로고    scopus 로고
    • Interaction of selection and recombination in the fixation of negative-epistatic genes
    • Michalakis Y., and Slatkin M. Interaction of selection and recombination in the fixation of negative-epistatic genes. Genetical Res. Cambridge 67 (1996) 257-269
    • (1996) Genetical Res. Cambridge , vol.67 , pp. 257-269
    • Michalakis, Y.1    Slatkin, M.2
  • 37
    • 0024760789 scopus 로고
    • Time for spreading of compensatory mutations under gene duplication
    • Ohta T. Time for spreading of compensatory mutations under gene duplication. Genetics 123 (1989) 579-584
    • (1989) Genetics , vol.123 , pp. 579-584
    • Ohta, T.1
  • 38
    • 34547954123 scopus 로고    scopus 로고
    • HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions
    • Olivares I., Mulky A., Boross P.I., Tözsér J., Kappes J.C., López-Galíndez C., and Menéndez-Arias L. HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions. J. Mol. Biol. 372 (2007) 369-381
    • (2007) J. Mol. Biol. , vol.372 , pp. 369-381
    • Olivares, I.1    Mulky, A.2    Boross, P.I.3    Tözsér, J.4    Kappes, J.C.5    López-Galíndez, C.6    Menéndez-Arias, L.7
  • 39
    • 0027996464 scopus 로고
    • Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA
    • Paillart JC., Marquet R., Skripkin E., Ehresmann B., and Ehresmann C. Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA. J. Biol. Chem. 269 (1994) 27486-27493
    • (1994) J. Biol. Chem. , vol.269 , pp. 27486-27493
    • Paillart, JC.1    Marquet, R.2    Skripkin, E.3    Ehresmann, B.4    Ehresmann, C.5
  • 40
    • 0033980890 scopus 로고    scopus 로고
    • Comparative sequence analysis and patterns of covariation in RNA secondary structures
    • Parsch J., Braverman J.M., and Stephan W. Comparative sequence analysis and patterns of covariation in RNA secondary structures. Genetics 154 (2000) 909-921
    • (2000) Genetics , vol.154 , pp. 909-921
    • Parsch, J.1    Braverman, J.M.2    Stephan, W.3
  • 41
    • 0029896552 scopus 로고    scopus 로고
    • Waiting for a compensatory mutation: phase zero of the shifting-balance process
    • Phillips P.C. Waiting for a compensatory mutation: phase zero of the shifting-balance process. Genetical Res. Cambridge 67 (1996) 271-283
    • (1996) Genetical Res. Cambridge , vol.67 , pp. 271-283
    • Phillips, P.C.1
  • 43
    • 0029784930 scopus 로고    scopus 로고
    • The rate of compensatory evolution
    • Stephan W. The rate of compensatory evolution. Genetics 144 (1996) 419-426
    • (1996) Genetics , vol.144 , pp. 419-426
    • Stephan, W.1
  • 44
    • 0027164566 scopus 로고
    • RNA folding in Drosophila shows a distance effect for compensatory fitness interaction
    • Stephan W., and Kirby D.A. RNA folding in Drosophila shows a distance effect for compensatory fitness interaction. Genetics 135 (1993) 97-103
    • (1993) Genetics , vol.135 , pp. 97-103
    • Stephan, W.1    Kirby, D.A.2
  • 45
    • 0026757625 scopus 로고
    • Structural and thermodynamic analysis of compensating mutations within the core of chicken egg-white lysozyme
    • Wilson K.P., Malcolm B.A., and Matthews B.W. Structural and thermodynamic analysis of compensating mutations within the core of chicken egg-white lysozyme. J. Biol. Chem. 267 (1992) 10842-10849
    • (1992) J. Biol. Chem. , vol.267 , pp. 10842-10849
    • Wilson, K.P.1    Malcolm, B.A.2    Matthews, B.W.3
  • 46
    • 0001771498 scopus 로고
    • Evolution in Mendelian populations
    • Wright S. Evolution in Mendelian populations. Genetics 16 (1931) 97-159
    • (1931) Genetics , vol.16 , pp. 97-159
    • Wright, S.1
  • 47
    • 0037244097 scopus 로고    scopus 로고
    • pistillata-5, an Arabidopsis B class mutant with strong defects in petal but not in stamen development
    • Yang Y., Xiang H., and Jack T. pistillata-5, an Arabidopsis B class mutant with strong defects in petal but not in stamen development. Plant J. 33 (2003) 177-188
    • (2003) Plant J. , vol.33 , pp. 177-188
    • Yang, Y.1    Xiang, H.2    Jack, T.3
  • 48
    • 6644223187 scopus 로고
    • Protein structure relationships revealed by mutational analysis
    • Yanofsky C., Horn V., and Thorpe D. Protein structure relationships revealed by mutational analysis. Science 146 (1964) 1593-1594
    • (1964) Science , vol.146 , pp. 1593-1594
    • Yanofsky, C.1    Horn, V.2    Thorpe, D.3


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