Synthesis, glycosylation and rapid secretion of a glycoprotein by Achlya, a primitive eucaryote.
Biochim Biophys Acta
; 674(1): 105-17, 1981 Apr 17.
Article
em En
| MEDLINE
| ID: mdl-7236724
ABSTRACT
Achlya ambisexualis, a water mold, secretes several glycoproteins during exponential growth. Among these is a major protein of 39 000 daltons (protein A-39) which is secreted very rapidly. Protein A-39 is detected among the soluble cellular proteins labeled for 5 min. However, after longer labeling times, an additional 95 000 dalton glycoprotein was immunoprecipitated from among the cytoplasmic proteins by antiserum against protein A-39. This antiserum reacted with a single 37 000 dalton protein from the in vitro translation products of poly(A)-containing RNA in a wheat germ cell-free system which is cleaved to a faster moving component in the presence of dog pancreatic membranes. Immunoprecipitated, chain-completion products of polysomes also show a 37 000 dalton peptide which does not bind to lectins, indicating absence of co-translational cleavage and glycosylation. Tunicamycin inhibits the appearance of the 95 000 dalton protein. Several immunoprecipitable proteins, including protein A-39, having sizes identical to the secretory proteins accumulate in the cytoplasm in the presence of this inhibitor. A short pulse with [3H]glucosamine followed by a chase showed that incorporation in protein A-39 increases while that in 95 000 dalton protein is decreasing. These results suggest that the 95 000 dalton glycoprotein may serve as a glycosyl donor to secretory protein A-39.
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Base de dados:
MEDLINE
Assunto principal:
Oomicetos
/
Proteínas Fúngicas
/
Glicoproteínas
/
Fungos
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1981
Tipo de documento:
Article