Conserved sequences flank variable tandem repeats in two alleles of the G surface protein of Paramecium primaurelia.
We describe the cloning and the sequencing of a macronuclear DNA fragment of Paramecium primaurelia, strain 168, encompassing the entire coding region of the 168G surface protein gene. Comparison of its nucleotide and its deduced amino acid sequences to those of the allelic surface protein 156G, previously described, reveals the rigorous conservation of a highly periodic structure. This structure is based on the presence of 37 periods of about 75 residues, each period containing eight cysteine residues. The differences between the two proteins are clustered in the central part of the sequence, which is itself made of quasi-identical tandem repeats. We propose that these repeats constitute the domain exposed on the surface of the cells and present the characteristics of concerted evolution.
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Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003545:Cysteine; D005796:Genes; D008562:Membrane Glycoproteins / Q000235:genetics*; D008969:Molecular Sequence Data; D010247:Paramecium / Q000235:genetics*; D015800:Protozoan Proteins / Q000235:genetics*; D012091:Repetitive Sequences, Nucleic Acid; D015183:Restriction Mapping
D008562:Membrane Glycoproteins; D015800:Protozoan Proteins; C051841:surface protein G, Paramecium; D003545:Cysteine