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c-type Lysozymes: what do their introns hide?

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      The introns of five c-type lysozymes were translated into amino acid sequences: parts of them corresponded to fragments of biologically active proteins. The amino acid sequences of translated introns seem to have a similar behavior as those arising from exons.

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      Most cited references 10

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      Gapped BLAST and PSI-BLAST a new generation of protein database search programs

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        Adaptive evolution in the stomach lysozymes of foregut fermenters.

        The convergent evolution of a fermentative foregut in two groups of mammals offers an opportunity to study adaptive evolution at the protein level. The appearance of this mode of digestion has been accompanied by the recruitment of lysozyme as a bacteriolytic enzyme in the stomach both in the ruminants (for example the cow) and later in the colobine monkeys (for example the langur). The stomach lysozymes of these two groups share some physicochemical and catalytic properties that appear to adapt them for functioning in the stomach fluid. To examine the basis for these shared properties, we sequenced langur stomach lysozyme and compared it to other lysozymes of known sequence. Tree analysis suggest that, after foregut fermentation arose in monkeys, the langur lysozyme gained sequence similarity to cow stomach lysozyme and evolved two times faster than the other primate lysozymes. This rapid evolution, coupled with functional and sequence convergence upon cow stomach lysozyme, could imply that positive darwinian selection has driven about 50% of the evolution of langur stomach lysozyme.
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          Evolution of stomach lysozyme: the pig lysozyme gene.

           J. Yu,  Jennifer Irwin (1996)
          The acquisition of an efficient stomach lysozyme is associated with the success of the ruminants. Advanced ruminants, such as cow, sheep, and deer, have approximately 10 lysozyme genes, some of which are expressed and function in the stomach and some which are expressed and function in nonstomach tissues (e.g., trachea or kidney). The pig possesses a single conventional lysozyme c gene that is expressed in both stomach and nonstomach tissues, and in this respect is similar to what was thought to exist in the early artiodactyl, before the acquisition of the ruminant lifestyle. To better understand the genetic events that occurred early in the origin and evolution of stomach lysozyme, we have isolated and characterized the pig lysozyme gene. The pig lysozyme gene is similar in size to that of other mammalian species, and both stomach and nonstomach expression utilize the same promoter. All the duplications of the ruminant lysozyme gene occurred after the divergence of the pig lineage from the lineage leading to the advanced ruminants. Comparison of the nucleotide sequence of the coding region of mature stomach lysozymes from advanced ruminants and pig revealed no change in the rate of synonymous substitutions. Comparison of the numbers of nonsynonymous and synonymous substitutions provides evidence for positive selection along the early ruminant lineage. These results indicate that changes in selective pressure, and not mutation rate, account for the changes in rates of stomach lysozyme evolution.

            Author and article information

            [1 ]Molécules de Communication, Museum National d'Histoire Naturelle, 63 rue Buffon, F 75005 Paris, France
            Author notes
            [* ]Corresponding author's e-mail address: pierre.jolles@
            (View ORCID Profile)
            ScienceOpen Research
            08 October 2014
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            1928:XE 10.14293/S2199-1006.1.SOR-LIFE.AJNDRN.v1
            © 2014 Pierre Jollès.

            This work has been published open access under Creative Commons Attribution License CC BY 4.0 , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Conditions, terms of use and publishing policy can be found at .

            Figures: 1, Tables: 2, References: 10, Pages: 3
            Original article

            Life sciences

            enzymes, exons, translation, introns, lysozymes


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