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001-es BibID:	BIBFORM045833
035-os BibID:	PMID:2120108
Első szerző:	Penyige András (molekuláris genetikus)
Cím:	ADP-ribosylation of membrane proteins of Streptomyces griseus strain 52-1 / Penyige, A., Barabas, Gy., Szabo, I., Ensign, J. C.
Dátum:	1990
ISSN:	0378-1097
Megjegyzések:	Membranes purified from cells of Streptomyces griseus strain 52-1 possess and ADP-ribosyltransferase acrivity. The enzyme transfers the DP-ribose moiety of NAD to one major membrane protein of Mr 32000 and 2?3 minot proteins of larger molecular weights. The effects of inhibitors on the ADP-ribosyltransferase activity proves that the reaction is enzymatic and suggests that the enzyme ADP-ribosylates the guanidine group of arginine. The kinetics of liberation of ADP-ribose during alkaline hydrolysis of the modified proteins is consistent with the arginine-ADP-ribose bond. This is the first report of ADP-ribosylation of proteins in a Gram-positive bacterium.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban ADP-ribosylation NAD-glycohydrolase Protein modification Streptomyces griseus
Megjelenés:	Fems Microbiology Letters. - 57 : 3 (1990), p. 293-297. -
További szerzők:	Barabás György (1933-) (sejtbiológus, molekuláris genetikus) Szabó I. Ensign, J. C.
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001-es BibID:	BIBFORM046866
Első szerző:	Penyige András (molekuláris genetikus)
Cím:	The possible role of ADP ribosylation in physiological regulation of sporulation in Streptomyces griseus / Penyige, A., Vargha, G., Ensign, J. C., Barabás, G.
Dátum:	1992
ISSN:	0378-1119
Megjegyzések:	The role of ADP ribosylation of proteins in the physiological regulation of sporulation in Streptomyces griseus was studied. We report here that both the activity of NAD+: arginine ADP-ribosyltransferase (ADPRT) and the pattern of ADP-ribosylated proteins showed characteristic changes during the life cycle in S. griseus 2682. Analysis off ADP-ribosylated proteins revealed that in a nonsporulating mutant of the parental wild-type (wt) strain (Bld7 mutant), both the activity of ADPRT and the pattern of ADP-ribosylated proteins were different from those of the parental strain. Addition of 3-aminobenzamide (3AB), the most potent inhibitor of ADPRT, inhibited sporulation of S. griseus 2682 and the A-factor (AF)-induced sporulation of S. griseus Bld7, but in both cases the inhibitory effect of 3AB was strictly age-dependent. Using [alpha-32P]GTP, we have demonstrated the presence of GTP-binding proteins in purified cell membranes of S. griseus 2682 and S. griseus Bld7. The same GTP-binding proteins were observed in Bld7 and the wt. AF stimulated the basal GTPase activity of cell membranes of S. griseus 2682 in a concentration-dependent manner, suggesting that GTP-binding proteins might be involved in the AF-induced sporulation process.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Gene. - 115 : 1-2 (1992), p. 181-185. -
További szerzők:	Vargha G. Ensign, J. C. Barabás György (1933-) (sejtbiológus, molekuláris genetikus)
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001-es BibID:	BIBFORM046862
Első szerző:	Penyige András (molekuláris genetikus)
Cím:	Modification of Glutamine Synthetase in Streptomyces griseus by ADP-Ribosylation and Adenylylation / Penyige, A., Kalmanczhelyi, A., Sipos, A., Ensign, J. C., Barabas, G.
Dátum:	1994
ISSN:	0006-291X
Megjegyzések:	Addition of NH+4 to Streptomyces griseus 2682 cells grown in NO?3 containing medium resulted in a rapid decline in glutamine synthetase activity due to covalent modification of the enzyme. The NH+4 promoted inactivation of the enzyme was inhibited by the ADP-ribosyltransferase inhibitor 3-methoxybenzamide. In the presence of ADP-ribosyltransferase activity the purified glutamine synthetase was also inhibited by NAD+ in a concentration-dependent manner. ADP-ribosylation of glutamine synthetase was demonstrated in vitro by showing the incorporation of labeled ADP-ribose from [?-32P]NAD+ into glutamine synthetase subunits. Beside ADP-ribosylation, adenylylation of glutamine synthetase was also shown in S. griseus since phosphodiesterase I treatment reactivated the enzyme in crude extracts of NH+4-shocked cells. Glutamine synthetase was also inhibited and modified by ATP in crude cellular extracts. These results suggest that in S. griseus 2682 ADP-ribosylation of glutamine synthetase could be an alternative modification to adenylylation to regulate glutamine synthetase activity.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Biochemical And Biophysical Research Communications. - 204 : 2 (1994), p. 598-605. -
További szerzők:	Kálmánczhelyi Attila Sipos Anikó Ensign, J. C. Barabás György (1933-) (sejtbiológus, molekuláris genetikus)
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