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      c-type Lysozymes: what do their introns hide?

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      1 , *

      ScienceOpen Research

      ScienceOpen

      Life sciences, Lysozymes, Introns, Translation, Exons, Enzymes

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          Abstract

          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 9

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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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            The human lysozyme gene. Sequence organization and chromosomal localization

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              Evolution of the bovine lysozyme gene family: changes in gene expression and reversion of function.

              Recruitment of lysozyme to a digestive function in ruminant artiodactyls is associated with amplification of the gene. At least four of the approximately ten genes are expressed in the stomach, and several are expressed in nonstomach tissues. Characterization of additional lysozymelike sequences in the bovine genome has identified most, if not all, of the members of this gene family. There are at least six stomachlike lysozyme genes, two of which are pseudogenes. The stomach lysozyme pseudogenes show a pattern of concerted evolution similar to that of the functional stomach genes. At least four nonstomach lysozyme genes exist. The nonstomach lysozyme genes are not monophyletic. A gene encoding a tracheal lysozyme was isolated, and the stomach lysozyme of advanced ruminants was found to be more closely related to the tracheal lysozyme than to the stomach lysozyme of the camel or other nonstomach lysozyme genes of ruminants. The tracheal lysozyme shares with stomach lysozymes of advanced ruminants the deletion of amino acid 103, and several other adaptive sequence characteristics of stomach lysozymes. I suggest here that tracheal lysozyme has reverted from a functional stomach lysozyme. Tracheal lysozyme then represents a second instance of a change in lysozyme gene expression and function within ruminants.
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                Author and article information

                Contributors
                (View ORCID Profile)
                Journal
                SOR-LIFE
                ScienceOpen Research
                ScienceOpen
                2199-1006
                08 October 2014
                : 0 (ID: 36f92335-138b-4943-bc61-f1922351138b )
                : 0
                : 1-3
                Affiliations
                [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@ 123456wanadoo.fr
                Article
                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 www.scienceopen.com .

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

                Life sciences

                lysozymes, introns, translation, exons, enzymes

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