Data/hora: 09/06/2024 11:29:05

Provedor de dados: | 74
País: | Brazil
Título: | The prion protein and New World primate phylogeny
Autores: | Schneider,Igor; Schneider,Horacio; Schneider,Maria Paula; Silva,Artur.
Data: | 2004-01-01
Ano: | 2004
Palavras-chave: | Prion protein; New World monkeys; Molecular phylogeny.
Resumo: | The PrP C prion protein contains 250 amino acids with some variation among species and is expressed in several cell types. PrP C is converted to PrP Sc by a post-translational process in which it acquires amino acid sequences of three-dimensional conformation of beta-sheets. Variations in the prion protein gene were observed among 16 genera of New World primates (Platyrrhini), and resulted in amino acid substitutions when compared with the human sequence. Seven substitutions not yet described in the literature were found: W -&gt; R at position 31 in Cebuella, T -&gt; A at position 95 in Cacajao and Chiropotes, N-&gt; S at position 100 in Brachyteles, L -&gt; Q at position 130 in Leontopithecus (in the sequence responsible for generating the beta-sheet 1), D -&gt; E at position 144 in Lagothrix (in the sequence responsible for the alpha-helix 1), D-&gt; G at position 147 in Saguinus (also located in the alpha-helix 1 region), and M -&gt; I at position 232 in Alouatta. The phylogenetic trees generated by parsimony, neighbor-joining and Bayesian analyses strongly support the monophyletic status of the platyrrhines, but did not resolve relationships among families. However, the results do corroborate previous findings, which indicate that the three platyrrhine families radiated rapidly from an ancient split.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572004000400007
Editor: | Sociedade Brasileira de Genética
Relação: | 10.1590/S1415-47572004000400007
Formato: | text/html
Fonte: | Genetics and Molecular Biology  v.27 n.4 2004
Fonte: | info:eu-repo/semantics/openAccess