Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The procyclin repertoire of Trypanosoma brucei - Identification and structural characterization of the Glu-Pro-rich polypeptides
Autore:
Acosta-Serrano, A; Cole, RN; Mehlert, A; Lee, MGS; Ferguson, MAJ; Englund, PT;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA JohnsHopkins Univ Baltimore MD USA 21205 l Chem, Baltimore, MD 21205 USA Univ Dundee, Dept Biochem, Dundee DD1 5EH, Scotland Univ Dundee Dundee Scotland DD1 5EH pt Biochem, Dundee DD1 5EH, Scotland NYU, Sch Med, Dept Pathol, New York, NY 10016 USA NYU New York NY USA 10016 U, Sch Med, Dept Pathol, New York, NY 10016 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 42, volume: 274, anno: 1999,
pagine: 29763 - 29771
SICI:
0021-9258(19991015)274:42<29763:TPROTB>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACIDIC REPETITIVE PROTEIN; AMANITIN-RESISTANT TRANSCRIPTION; 3'-UNTRANSLATED REGION; AFRICAN TRYPANOSOMES; TRANS-SIALIDASE; SURFACE-ANTIGEN; CULTURE FORMS; EXPRESSION; INSECT; GENES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Acosta-Serrano, A Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 MD 21205 USA
Citazione:
A. Acosta-Serrano et al., "The procyclin repertoire of Trypanosoma brucei - Identification and structural characterization of the Glu-Pro-rich polypeptides", J BIOL CHEM, 274(42), 1999, pp. 29763-29771

Abstract

The surface of the insect stages of the protozoan parasite Trypanosoma brucei is covered by abundant glycosyl phosphatidylinositol (GPI)-anchored glycoproteins known as procyclins. One type of procyclin, the EP isoform, is predicted to have 22-30 Glu-Pro (EP) repeats in its C-terminal domain and isencoded by multiple genes. Because of the similarity of the EP isoform sequences and the heterogeneity of their GPI anchors, it has been impossible to separate and characterize these polypeptides by standard protein fractionation techniques. To facilitate their structural and functional characterization, we used a combination of matrix-assisted laser desorption ionizationand electrospray mass spectrometry to analyze the entire procyclin repertoire expressed on the trypanosome cell. This analysis, which required removal of the GPI anchors by aqueous hydrofluoric acid treatment and cleavage ataspartate-proline bonds by mild acid hydrolysis, provided precise information about the glycosylation state and the number of Glu-Pro repeats in these proteins. Using this methodology we detected in a T. brucei clone the glycosylated products of the EP3 gene and two different products of the EP1 gene (EP1-1 and EP1-2). Furthermore, only low amounts of the nonglycosylated products of the GREET and EP2 genes were detected. Because all procyclin genes are transcribed polycistronically, the latter finding indicates that the expression of the GREET and ER2 genes is post-transcriptionaly regulated. This is the first time that the whole procyclin repertoire from procyclic trypanosomes has been characterized at the protein level.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 22:57:39