The Divergence of Species-Specific Abalone Sperm Lysins is Promoted by Positive Darwinian Selection.

Recognition by sperm lysin of the egg vitelline envelope may be one component in determining the species-specificity of fertilization in abalones. The amino acid sequences of lysin proteins of seven California abalone species were deduced from the cDNA sequences. This is the first extensive comparison of a gamete recognition protein from congeneric species. Each prelysin has a highly conserved signal peptide of 18 amino acids, followed by a mature sequence of 136-138 residues. Of 136 aligned positions, 68 have the same amino acid in all seven sequences. The % identity relative to the red abalone lysin sequence is: white 90%, flat 83%, pinto 82%, pink 78%, black 71%, and green 65%. Hydropathy plots and a distance tree of the seven lysins show that red, white, and flat lysins are more closely related to each other than to the lysins of the other four species. A hypervariable, species-specific, domain exists in all sequences between positions 2-12. Amino acid replacements between any two lysins are mostly nonconservative. Analysis of the cDNA sequences shows the number of nonsynonymous substitutions (amino acid altering) exceeds the number of synonymous substitutions (silent) in 20 of the 21 pairwise comparisons of the seven sequences, indicating that positive Darwinian selection must promote the divergence of lysin sequences.

[1]  M. Kreitman,et al.  Adaptive protein evolution at the Adh locus in Drosophila , 1991, Nature.

[2]  W. Fitch,et al.  Positive Darwinian evolution in human influenza A viruses. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[3]  A. Hughes,et al.  Circumsporozoite protein genes of malaria parasites (Plasmodium spp.): evidence for positive selection on immunogenic regions. , 1991, Genetics.

[4]  Ld Brown,et al.  Genetic variation and population stucture in the blacklip abalone, Haliotis rubra , 1991 .

[5]  N. Johnsson,et al.  Protein‐protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11. , 1990, The EMBO journal.

[6]  M. Nei,et al.  Positive Darwinian selection promotes charge profile diversity in the antigen-binding cleft of class I major-histocompatibility-complex molecules. , 1990, Molecular biology and evolution.

[7]  C. Chothia,et al.  The structure of protein-protein recognition sites. , 1990, The Journal of biological chemistry.

[8]  C. Stout,et al.  Species-specific sequences of abalone lysin, the sperm protein that creates a hole in the egg envelope. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[9]  C. Stout,et al.  Diffraction quality crystals of lysin from spermatozoa of the red abalone (Haliotis rufescens). , 1990, The Journal of biological chemistry.

[10]  M. Frohman.  4 – RACE: RAPID AMPLIFICATION OF cDNA ENDS , 1990 .

[11]  M. Nei,et al.  Positive darwinian selection observed at the variable-region genes of immunoglobulins. , 1989, Molecular biology and evolution.

[12]  R. Yanagimachi,et al.  Cross-fertilization between Syrian and Chinese hamsters. , 1989, The Journal of experimental zoology.

[13]  M. Nei,et al.  Nucleotide substitution at major histocompatibility complex class II loci: evidence for overdominant selection. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[14]  M. Nei,et al.  Pattern of nucleotide substitution at major histocompatibility complex class I loci reveals overdominant selection , 1988, Nature.

[15]  M. O'Rand.  Sperm-egg recognition and barriers to interspecies fertilization. , 1988, Gamete research.

[16]  P. Chomczyński,et al.  Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. , 1987, Analytical biochemistry.

[17]  Jeremy D. Prince,et al.  Experimental evidence for limited dispersal of haliotid larvae (genus Haliotis; Mollusca: Gastropoda) , 1987 .

[18]  V. Vacquier,et al.  Fusion of liposomes induced by a cationic protein from the acrosome granule of abalone spermatozoa. , 1986, Biochemistry.

[19]  M. Nei,et al.  Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. , 1986, Molecular biology and evolution.

[20]  T. Cooper.  Sperm-Egg Fusion , 1986 .

[21]  G. von Heijne,et al.  Signal sequences: The limits of variation , 1985 .

[22]  C. Luo,et al.  A new method for estimating synonymous and nonsynonymous rates of nucleotide substitution considering the relative likelihood of nucleotide and codon changes. , 1985, Molecular biology and evolution.

[23]  代谷 陽子,et al.  Fine Structure of the Spermatozoon in the Japanese Abalone, Haliotis discus , 1983 .

[24]  Richard Earl Dickerson,et al.  Hemoglobin : structure, function, evolution, and pathology , 1983 .

[25]  V. Vacquier,et al.  A protein from abalone sperm dissolves the egg vitelline layer by a nonenzymatic mechanism. , 1982, Developmental biology.

[26]  R. Doolittle,et al.  A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.

[27]  K. Kyozuka,et al.  Cross fertilization between sea urchin eggs and oyster spermatozoa , 1982 .

[28]  V. Vacquier,et al.  Morphology of abalone spermatozoa before and after the acrosome reaction. , 1980, Journal of ultrastructure research.

[29]  R. Summers,et al.  Primary gamete binding. Quantitative determination of its specificity in echinoid fertilization. , 1976, Experimental cell research.

[30]  R. Summers,et al.  Species-specificity of acrosome reaction and primary gamete binding in echinoids. , 1975, Experimental cell research.

[31]  K. Haino-fukushima.  Studies on the egg-membrane lysin of Tegula pfeifferi. The reaction mechanism of the egg-membrane lysin. , 1974, Biochimica et biophysica acta.