ADP-ribosylation of an approximately 70-kilodalton protein of Klebsiella pneumoniae.
AUTOR(ES)
Geipel, U
RESUMO
An approximately 70-kDa protein in the culture supernatant of a human pathogenic strain of Klebsiella pneumoniae was labeled in the presence of [32P-adenylate]NAD. Labeling was significantly increased by the addition of dithiothreitol ( > 1 mM) but prevented by treatment of the culture supernatant for 3 min at 56 degrees C. The addition of unlabeled NAD, but not of ADP-ribose, blocked labeling of the approximately 70-kDa protein. The radioactive label was released by formic acid but not by HgCl2 (1 mM) or neutral hydroxylamine (0.5 M). The addition of homogenates of human platelets, human neutrophils, rat brain, rat lung, or rat spleen tissues to the culture supernatant did not induce labeling of eukaryotic proteins. The data indicate that the K. pneumoniae strain produces ADP-ribosyltransferase which modifies an endogenous protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=173984Documentos Relacionados
- Saccharomyces cerevisiae Gcs1 is an ADP-ribosylation factor GTPase-activating protein.
- Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides.
- Agonist-induced ADP-ribosylation of a cytosolic protein in human platelets.
- Endogenous ADP-ribosylation of proteins in Mycobacterium smegmatis.
- Stimulation of endogenous ADP-ribosylation by brefeldin A.
