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Posttranslational modifications of alpha- and beta-tubulin in Giardia lamblia, an ancient eukaryote.
Weber, K; Schneider, A; Westermann, S; Müller, N; Plessmann, U.
Afiliação
  • Weber K; Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Göttingen, Germany.
FEBS Lett ; 419(1): 87-91, 1997 Dec 08.
Article em En | MEDLINE | ID: mdl-9426225
ABSTRACT
Tubulin of Giardia lamblia, a representative of the oldest eukaryotes, was screened for posttranslational modifications. Mass spectrometry of the carboxy-terminal peptides documents a large number of variants. Both alpha- and beta-tubulin show polyglycylation with up to 20 and 15 extra glycyl residues respectively. Minor variants show a low level of glutamylation without or with glycylation. The glutamylation-specific antibody GT335 detects alpha- and beta-tubulin in immunoblots. The terminal tyrosine is fully retained in alpha-tubulin, which is completely acetylated at Lys-40. Thus except for the detyrosination/tyrosination cycle all posttranslational modifications known for higher eukaryotes are already present in Giardia.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tubulina (Proteína) / Processamento de Proteína Pós-Traducional / Giardia lamblia Limite: Animals Idioma: En Revista: FEBS Lett Ano de publicação: 1997 Tipo de documento: Article País de afiliação: Alemanha
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tubulina (Proteína) / Processamento de Proteína Pós-Traducional / Giardia lamblia Limite: Animals Idioma: En Revista: FEBS Lett Ano de publicação: 1997 Tipo de documento: Article País de afiliação: Alemanha