ADP-ribosylation of p21ras and related proteins by Pseudomonas aeruginosa exoenzyme S
نویسندگان
چکیده
منابع مشابه
ADP-ribosylation of p21ras and related proteins by Pseudomonas aeruginosa exoenzyme S.
Pseudomonas aeruginosa exoenzyme S ADP-ribosylates p21ras and several related proteins. ADP-ribosylation of p21ras does not alter interactions with guanine nucleotides. The ras-related GTP-binding proteins, including Rab3, Rab4, Ral, Rap1A, and Rap2, are also substrates; given these results, we propose a model for the role of exoenzyme S in pathogenesis.
متن کاملEcto-ADP-ribosyltransferase activity of Pseudomonas aeruginosa exoenzyme S.
Pseudomonas aeruginosa produces two ADP-ribosyltransferases, exotoxin A and exoenzyme S (ExoS). Although the physiological target protein remains to be defined, ExoS has been shown to ADP-ribosylate several eukaryotic proteins in vitro, including vimentin and members of the family of low-molecular-weight GTP-binding proteins. Recently, ExoS ADP-ribosyltransferase activity has been detected in t...
متن کاملPseudomonas aeruginosa exoenzyme S is a biglutamic acid ADP-ribosyltransferase.
Kinetic analysis of two mutations within Pseudomonas aeruginosa exoenzyme S (ExoS) showed that a E379D mutation inhibited expression of ADP-ribosyltransferase activity but had little effect on the expression of NAD glycohydrolase activity while a E381D mutation inhibited expression of both activities. These data identify ExoS as a biglutamic acid ADP-ribosyltransferase, where E381 is the cataly...
متن کاملPurification of Pseudomonas aeruginosa exoenzyme S.
Pseudomonas aeruginosa produces two distinct ADP-ribosyl transferases, exotoxin A and exoenzyme S, which differ in a number of properties including substrate specificity. Exoenzyme S was purified from culture supernatants of P. aeruginosa DG1. The procedure for purification consists of four major steps: ammonium sulfate precipitation, anion-exchange chromatography on DEAE-Sephacel, acetone prec...
متن کاملPseudomonas aeruginosa exoenzyme S is an adhesion.
Exoenzyme S from Pseudomonas aeruginosa has been studied as an adhesion for glycosphingolipids and buccal cells. Binding of exoenzyme S to gangliotriosylceramide (GalNAc beta 1-4Gal beta 1-4Glc beta 1-1Cer), gangliotetraosylceramide (Gal beta 1-3 GalNAcT beta 1-4 Gal beta 1-4Glc beta 1-1Cer), and lactosylceramide (Gal beta 1-4Glc beta 1-1Cer) separated on thin-layer chromatograms was observed. ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1991
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.59.11.4259-4262.1991