Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates
Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we cha...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2000 |
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| Umfang: |
12 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Journal of molecular evolution - 1971, 51(2000) vom: Jan., Seite 76-87 |
| Übergeordnetes Werk: |
volume:51 ; year:2000 ; month:01 ; pages:76-87 ; extent:12 |
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| 520 | |a Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. | ||
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(DE-627)NLEJ207112193 DE-627 ger DE-627 rakwb eng Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates 2000 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. Springer Online Journal Archives 1860-2002 Huang, Cheng-Han oth Liu, Zhi oth Apoil, Pol-André oth Blancher, Antoine oth in Journal of molecular evolution 1971 51(2000) vom: Jan., Seite 76-87 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:51 year:2000 month:01 pages:76-87 extent:12 http://dx.doi.org/10.1007/s002390010068 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 51 2000 1 76-87 12 |
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(DE-627)NLEJ207112193 DE-627 ger DE-627 rakwb eng Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates 2000 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. Springer Online Journal Archives 1860-2002 Huang, Cheng-Han oth Liu, Zhi oth Apoil, Pol-André oth Blancher, Antoine oth in Journal of molecular evolution 1971 51(2000) vom: Jan., Seite 76-87 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:51 year:2000 month:01 pages:76-87 extent:12 http://dx.doi.org/10.1007/s002390010068 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 51 2000 1 76-87 12 |
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(DE-627)NLEJ207112193 DE-627 ger DE-627 rakwb eng Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates 2000 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. Springer Online Journal Archives 1860-2002 Huang, Cheng-Han oth Liu, Zhi oth Apoil, Pol-André oth Blancher, Antoine oth in Journal of molecular evolution 1971 51(2000) vom: Jan., Seite 76-87 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:51 year:2000 month:01 pages:76-87 extent:12 http://dx.doi.org/10.1007/s002390010068 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 51 2000 1 76-87 12 |
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(DE-627)NLEJ207112193 DE-627 ger DE-627 rakwb eng Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates 2000 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. Springer Online Journal Archives 1860-2002 Huang, Cheng-Han oth Liu, Zhi oth Apoil, Pol-André oth Blancher, Antoine oth in Journal of molecular evolution 1971 51(2000) vom: Jan., Seite 76-87 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:51 year:2000 month:01 pages:76-87 extent:12 http://dx.doi.org/10.1007/s002390010068 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 51 2000 1 76-87 12 |
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(DE-627)NLEJ207112193 DE-627 ger DE-627 rakwb eng Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates 2000 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. Springer Online Journal Archives 1860-2002 Huang, Cheng-Han oth Liu, Zhi oth Apoil, Pol-André oth Blancher, Antoine oth in Journal of molecular evolution 1971 51(2000) vom: Jan., Seite 76-87 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:51 year:2000 month:01 pages:76-87 extent:12 http://dx.doi.org/10.1007/s002390010068 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 51 2000 1 76-87 12 |
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Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates |
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Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. |
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Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. |
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Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ207112193</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706221301.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s2000 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ207112193</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Sequence, Organization, and Evolution of Rh50 Glycoprotein Genes in Nonhuman Primates</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2000</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">12</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract. The human RHAG locus encodes Rh50 glycoprotein, a polytopic protein that modulates expression of Rh antigens carried by Rh30 polypeptides. Rh50 is almost invariant, whereas Rh30 shows high polymorphism. To assess the relative conservation and phylogenetic relationship of RHAG genes, we characterized their protein expression, transcript structure, genomic organization, and noncoding regions (promoter and introns) in seven nonhuman primate species. Western blot showed that only ape Rh50 glycoproteins are recognized by the antibody 2D10 specific for the human counterpart. Analysis of RHAG gene and its transcript showed a high degree of sequence identity and features of interspecific diversity. The nonhuman primate RHAG genes are highly similar in promoter region and identical in exon-intron organization. Genomic sequencing identified one retro-transposon–like element in intron 2 and three types of Alu elements in intron 4 and 9, with varying copies of minisatellites. Reconstruction of coding and noncoding sequence trees revealed concordances and discordances with regard to the branching of RHAG-like genes in higher primates. A joined tree of Rh50 glycoproteins and Rh30 polypeptides shows that the former evolved at a rate about two times slower than the latter. Statistical tests demonstrated that at least a portion of the RHAG gene was subjected to a positive selection during evolution of anthropoids.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Huang, Cheng-Han</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Liu, Zhi</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Apoil, Pol-André</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Blancher, Antoine</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of molecular evolution</subfield><subfield code="d">1971</subfield><subfield code="g">51(2000) vom: Jan., Seite 76-87</subfield><subfield code="w">(DE-627)NLEJ188994645</subfield><subfield code="w">(DE-600)1464309-1</subfield><subfield code="x">1432-1432</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:51</subfield><subfield code="g">year:2000</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:76-87</subfield><subfield code="g">extent:12</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/s002390010068</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">51</subfield><subfield code="j">2000</subfield><subfield code="c">1</subfield><subfield code="h">76-87</subfield><subfield code="g">12</subfield></datafield></record></collection>
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