Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A point mutation in an unusual Sec7 domain is linked to brefeldin A resistance in a Plasmodium falciparum line generated by drug selection
Autore:
Baumgartner, F; Wiek, S; Paprotka, K; Zauner, S; Lingelbach, K;
Indirizzi:
Univ Marburg, Fachbereich Biol, D-35032 Marburg, Germany Univ Marburg Marburg Germany D-35032 eich Biol, D-35032 Marburg, Germany
Titolo Testata:
MOLECULAR MICROBIOLOGY
fascicolo: 5, volume: 41, anno: 2001,
pagine: 1151 - 1158
SICI:
0950-382X(200109)41:5<1151:APMIAU>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUANINE-NUCLEOTIDE-EXCHANGE; ADP-RIBOSYLATION FACTOR; SECRETORY PATHWAY; PROTEIN-TRANSPORT; HOST ERYTHROCYTE; MALARIA PARASITE; STRUCTURAL BASIS; ARF GTPASE; BINDING; VIEW;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Lingelbach, K Univ Marburg, Fachbereich Biol, D-35032 Marburg, Germany Univ Marburg Marburg Germany D-35032 5032 Marburg, Germany
Citazione:
F. Baumgartner et al., "A point mutation in an unusual Sec7 domain is linked to brefeldin A resistance in a Plasmodium falciparum line generated by drug selection", MOL MICROB, 41(5), 2001, pp. 1151-1158

Abstract

The malaria parasite Plasmodium falciparum has an unusual organization of its secretory compartments. As an approach to a functional identification of auxiliary proteins involved in secretion, a parasite line was generated by drug selection that is resistant to brefeldin A, an inhibitor of the secretory pathway. In the resistant line, neither protein secretion nor parasite viability were affected by the drug. The analysis of a sec7 domain, a conserved structure of guanine nucleotide exchange factors (ARF-GEF) required for the activation of ADP-ribosylation factors, revealed a single methionine-isoleucine substitution in the resistant parasite line. ARF-GEFs are key molecules in the formation of transport vesicles and the main targets of brefeldin A. The methionine residue in this position of sec7 domains is highly conserved and confers brefeldin A sensitivity. Unlike other eukaryotes that have multiple ARF-GEFs, the plasmodial genome encodes a single sec7 domain. This domain shows a distinct structural difference to all sec7 domains analysed so far; two conserved subdomains that are essential for protein function are separated in the plasmodial protein by an insertion of 146 aminoacids.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 09:46:54