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1.

001-es BibID:BIBFORM045827
Első szerző:Barabás György (sejtbiológus, molekuláris genetikus)
Cím:Hormone-like factors influencing differentiation of Streptomyces cultures / Gy. Barabas, A. Penyige, T. Hirano
Dátum:1994
ISSN:0168-6445
Megjegyzések:Actinomycetes produce and export small autoregulatory molecules, which act like prokaryotic hormones. They can promote or induce sporulation, aerial hyphae formation and antibiotic production. The mode of action of the gamma-lactone AF is partly elucidated, those of the others are not known. These autoregulators (hormones) are effective if exogenously added to culture in proper time of the life cycle and in very low concentration. Since they influence the length of idiophase where secondary metabolites are produced their study may have pratical importance.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
A-FACTOR
A-FACTOR-BINDING PROTEIN;
AUTOREGULATOR
GTP-ASE ACTIVITY
STREPTOMYCES GRISEUS
Megjelenés:Fems Microbiology Reviews. - 14 : 1 (1994), p. 75-82. -
További szerzők:Penyige András (1954-) (molekuláris genetikus) Hirano, Tadashi
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2.

001-es BibID:BIBFORM004678
035-os BibID:(scopus)0035153667 (wos)000171533400007
Első szerző:Barabás György (sejtbiológus, molekuláris genetikus)
Cím:N-Alkane uptake and utilisation by Streptomyces strains / Barabas, G., Vargha, G., Szabo, I. M., Penyige, A., Damjanovich, S., Szollosi, J., Matko, J., Hirano, T., Matyus, A., Szabo, I.
Dátum:2001
Megjegyzések:Streptomyces strains isolated from the Kuwait Burgan oil field were defined as S. griseoflavus, S. parvus, and S. plicatus utilised n-hexadecane, n-octadecane (purified fractions of mineral oil), kerosene, and crude oil as sole carbon and energy sources. The strains were incubated with n-alkanes and increase of the fatty acid content with chain length equivalent to the employed n-alkanes was observed. Signal transducing GTP-binding proteins (GBPs) play an important role in n-alkane uptake in streptomycetes. Specific activators of GBPs increased the uptake of hydrocarbons. Using the hydrophobic fluorescent dye diphenylhexatrien (DPH) as a probe, it was found that the microviscosity of the hydrophobic inner region of the cellular membrane is significantly lower in hydrocarbon utilisers than in non-utilisers. This difference probably reflects differences in the fatty acid composition of the strains. When cultures were grown in n-alkane containing media, electron microscopy revealed that the hydrocarbon utilisers showed less-electron dense areas as inclusions in the cytoplasm. Soil samples inoculated with Streptomyces strains eliminated hydrocarbons much faster than those not containing these strains, serving as control. When inorganic medium was supplied with n-hexadecane-1-14C as sole carbon and energy source, radioactive CO2 was detected. Since streptomycetes have not been used until now for oil elimination, though they are known as abundant soil bacteria tolerating extreme conditions, their possible use for bioremediation of hydrocarbon contaminated soils is discussed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Alkanes
analogs and derivatives
analysis
Biodegradation
Cell Membrane
Cell Membrane Permeability
chemistry
Cytoplasm
Diphenylhexatriene
Dyes
Fatty Acids
Fluorescent Dyes
genetics
GTP-Binding Proteins
Human
Hungary
Hydrocarbons
metabolism
Microscopy
physiology
Streptomyces
Support,Non-U.S.Gov't
ultrastructure
Megjelenés:Antonie Van Leeuwenhoek. - 79 : 3-4 (2001), p. 269-276. -
További szerzők:Vargha György (1951-) (orvos) Szabó István M. Penyige András (1954-) (molekuláris genetikus) Damjanovich Sándor (1936-2017) (biofizikus) Szöllősi János (1953-) (biofizikus) Matkó János (1952-) (biológus) Hirano, Tadashi Mátyus Anita Szabó István
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3.

001-es BibID:BIBFORM046861
Első szerző:Deák Eleonóra
Cím:Membrane-bound and extracellular beta-lactamase production with developmental regulation in Streptomyces griseus NRRL B-2682 / Deak, E., Szabo, I., Kalmaczhelyi, A., Gal, Z., Barabas, G., Penyige, A.
Dátum:1998
ISSN:1350-0872 1465-2080
Megjegyzések:A new type of beta-lactamase has been isolated and characterized in Streptomyces griseus NRRL B-2682. The enzyme has membrane-bound and extracellular forms. Biochemical characterization of some of the properties of the enzyme showed that it belongs to the class A group of penicillinases. Comparison of the membrane-bound and extracellular forms of the beta-lactamases suggests that they seem to be differently processed forms of the same enzyme. The N-terminal amino acid sequence of the extracellular form of the beta-lactamase showed a high degree of similarity to a D-aminopeptidase of another Streptomyces griseus strain. Secretion of the beta-lactamase was affected by the differentiation state of the strain since in spontaneous non-sporulating mutants only the membrane-bound form was present. In accordance with this when sporulation of the wild-type strain was inhibited it failed to secrete extracellular beta-lactamase. Addition of globomycin to the non-sporulating cells liberated the enzyme from the membrane, indicating that the protein is processed normally by signal peptidase II and a glyceride-thioether group, together with a fatty acid amide-linkage, is responsible for the attachment of the enzyme to the cellular membrane. Under sporulation-repressed conditions addition of peptidoglycan fragments and analogues or inhibition of cell wall biosynthesis by penicillin-G induced beta-lactamase secretion and also restored sporulation both in solid and submerged cultures. These results confirm that beta-lactamase secretion is tightly coupled to the sporulation process in S. griseus.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Microbiology (Reading, England). - 144 : 8 (1998), p. 2169-2177. -
További szerzők:Szabó István (1950-) (sejtbiológus, molekuláris genetikus) Kálmánczhelyi Attila Gál Zsuzsanna (1959-) (vegyész) Barabás György (1933-) (sejtbiológus, molekuláris genetikus) Penyige András (1954-) (molekuláris genetikus)
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4.

001-es BibID:KLTEbibl001439
Első szerző:Dinya Zoltán (vegyész)
Cím:Production of a Streptomycin-Park Nucleotide Complex by Streptimyces opiseus. / Dinya Zoltán, Szabó G., Barabás György, Penyige András, Szabó I.
Dátum:1989
ISSN:0066-4804
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Antimicrobial Agents and Chemotherapy. - 33 : 1 (1989) 58-62. -
További szerzők:Szabó G. Barabás György (1933-) (sejtbiológus, molekuláris genetikus) Penyige András (1954-) (molekuláris genetikus) Szabó I.
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5.

001-es BibID:BIBFORM045829
035-os BibID:PMID:1485715
Első szerző:Fülöp Tamás Jr
Cím:Transmembrane signaling changes with aging / T. Fülöp Jr, Gy. Barabás, Z. Varga, J. Csongor, M. Hauck, S. Szücs, I. Seres, A. Mohacsi, D. Kékessy, J. P. Despont, L. Robert, A. Penyige
Dátum:1992
ISSN:0077-8923
Megjegyzések:Altered immune response and transmembrane signaling with aging has previously been demonstrated. The aim of the present study was to characterize PMNLs and lymphocyte G proteins and to determine whether their relative amounts are altered with aging. First we studied the effects of FMLP on PMNLs IP3 formation. It was found that in any group of elderly the PMNLs IP3 formation was significantly decreased compared to that of young subjects. In FMLP receptor binding affinity no measurable difference exists in either low- or high-affinity FMLP receptors. The autoradiogram of 32P-ADP-ribosylated proteins by CT in lymphocytes of young individuals showed a major polypeptide of 40 kDa, and two much less prevalent components of 52 and 45 kDa. In contrast, in lymphocytes of elderly subjects the major polypeptide was 45 kDa, and the two others were very weakly labeled. In PMNLs, CT labeled the 45-kDa band quite strongly, mainly in the elderly, and the 52- and 40-kDa bands were very weakly labeled, mainly in young subjects. When PT was used, no age-related pattern changes could be demonstrated, while differences could be observed between the two types of cells.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
AGE-RELATED DECLINE
PHOSPHATIDYLINOSITOL BREAKDOWN
LYMPHOCYTES-T
G-PROTEIN
Megjelenés:Annals of The New York Academy of Sciences. - 673 (1992), p. 165-171. -
További szerzők:Barabás György (1933-) (sejtbiológus, molekuláris genetikus) Varga Z. Csongor József Hauck Mátyás (biokémikus) Szűcs Sándor (1958-) (biokémikus, vegyész) Seres Ildikó (1954-) (biokémikus) Mohácsi A. (orvos) Kékessy D. Despont, J. P. Robert, Ladislas Penyige András (1954-) (molekuláris genetikus)
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6.

001-es BibID:BIBFORM046864
Első szerző:Fülöp Tamás (népegészségügyi szakember, egészségfejlesztő)
Cím:Age-dependent changes in transmembrane signalling : identification of G proteins in human lymphocytes and polymorphonuclear leukocytes / Fulop Tamás, Barabas György, Varga Zsuzsa, József Csongor, Csabina Sándor, Szucs Sándor, Seres Ildikó, Szikszay Edit, Jeney Zsolt, Penyige András
Dátum:1993
ISSN:0898-6568
Megjegyzések:In human neutrophils (PMNLs) we found that in the elderly IP3 formation was significantly decreased compared to that of young subjects. For FMLP receptor binding affinity and number no measurable differences occurred upon ageing, studying both the low or the high affinity receptors. The amount of ADP-ribosylated G proteins, catalysed by pertussis toxin (PT) or cholera toxin (CT), was significantly increased in PMNLs of the elderly. In lymphocytes, the PT-catalysed ADP ribosylation of G proteins was also increased with ageing, while the CT-catalysed ribosylation was decreased. The autoradiogram of [32P]ADP-ribosylated proteins by CT in lymphocytes of young individuals showed a major polypeptide of 40,000 M(r). In contrast, in lymphocytes of the elderly, the major polypeptide was 45,000 M(r). In PMNLs, CT labelled quite strongly the 45,000 M(r) band, mainly in the elderly. When PT was used, no age-related pattern changes could be demonstrated, while differences could be observed between the two types of cells. The use of antiserum P680 (G alpha common) showed no age-related pattern changes, while the intensity of the labelled proteins varies with age and cell type. The antiserum U46 (Go alpha) could identify in lymphocytes of young subjects two polypeptides 68,000 and 41,000 M(r). The prominent polypeptide in lymphocytes of the elderly was the 70,000 M(r) and no other polypeptides could be recognized. In PMNLs of young subjects the U46 and serum identified a range of species. In PMNLs of the elderly all these bands were weakly labelled. The present data indicate changes in the pattern and the quantity of G proteins in lymphocytes and PMNLs of elderly subjects.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cellular Signalling. - 5 : 5 (1993), p. 593-603. -
További szerzők:Barabás György (1933-) (sejtbiológus, molekuláris genetikus) Varga Zsuzsa (1951-) (biokémikus, nephrológus) József Csongor Csabina Sándor Szűcs Sándor (1958-) (biokémikus, vegyész) Seres Ildikó (1954-) (biokémikus) Szikszay Edit Jeney Zsolt Penyige András (1954-) (molekuláris genetikus)
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7.

001-es BibID:BIBFORM046865
Első szerző:Ochi, Kozo
Cím:The possible role of ADP-ribosylation in sporulation and streptomycin production by Streptomyces griseus / Ochi, K., Penyige, A., Barabás, Gy.
Dátum:1992
ISSN:0022-1287
Megjegyzések:Mutants resistant to 3-aminobenzamide, a known inhibitor of ADP-ribosyltransferase, were obtained from Streptomyces griseus IFO 13189, a streptomycin-producing strain. One (strain no. 4), which had significantly reduced ADP-ribosyltransferase activity, was analysed in detail. Mutant 4 displayed a conditional phenotype with respect to cultivation temperature. At 30 degrees C, it exhibited severely reduced ability to produce aerial mycelium (on solid medium) and submerged spores and streptomycin (in liquid culture), but this ability was fully restored at 25 degrees C. The mutant produced A-factor normally, regardless of cultivation temperature, and exhibited normal ability to accumulate ppGpp intracellularly. SDS-PAGE analyses of cellular proteins labelled by [32P]NAD revealed that an ADP-ribosylated protein with a molecular size of 44 kDa, which appeared in sporulating cultures of the parent strain, was missing from the mutant grown at the non-permissive temperature (30 degrees C). Genetic analysis showed that the aba mutation conferring resistance to 3-aminobenzamide was tightly linked to the altered phenotype. Failure to ADP-ribosylate certain cellular protein(s), presumably due to the aba mutation, may be responsible for impaired differentiation in this mutant.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of General Microbiology. - 138 : (Pt8) (1992), p. 1745-1750. -
További szerzők:Penyige András (1954-) (molekuláris genetikus) Barabás György (1933-) (sejtbiológus, molekuláris genetikus)
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8.

001-es BibID:BIBFORM047235
035-os BibID:(PMID)8800814
Első szerző:Penyige András (molekuláris genetikus)
Cím:Evidence of a role for NAD+-glycohydrolase and ADP-ribosyltransferase in growth and differentiation of Streptomyces griseus NRRL B-2682 : inhibition by m-aminophenylboronic acid / András Penyige, Eleonóra Deák, Attila Kálmánczhelyi, György Barabás
Dátum:1996
ISSN:1350-0872 1465-2080
Megjegyzések:m-Aminophenylboronic acid (APBA) inhibited the germination, growth and sporulation of Streptomyces griseus NRRL B-2682 in an age- and concentration-dependent manner in submerged and solid cultures. When added to cells or cell extracts it irreversibly inhibited NAD+-glycohydrolase and ADP-ribosyltransferase activity. ADP-ribosyltransferase was more sensitive, but inhibition was not complete, even in the presence of 10 mM APBA. The in vivo effects of the inhibitor correlated with its in vitro effect on ADP-ribosylation and on the profile of ADP-ribosylated endogenous proteins. The physiological importance of ADP-ribosyltransferase was supported by the observation that APBA strongly inhibited the growth of a non-sporulating and NAD+- glycohydrolase-negative mutant of the parental strain. The resistance of S. griseus NRRL B-2682 strains able to grow in the presence of APBA was due to permeability factors. A comparison of the ADP-ribosylated protein profiles of S. griseus NRRL B-2682 grown under various conditions showed similarities, but also specific differences. The results suggest that the ADP-ribosyltransferase of S. griseus NRRL B-2682 is an indispensable enzyme for growth and differentiation of the strain. It may regulate the activity of key enzymes or developmental proteins by responding to intra- and extracellular conditions.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Microbiology (Reading, England). - 142 : 8 (1996), p. 1937-1944. -
További szerzők:Deák Eleonóra Kálmánczhelyi Attila Barabás György (1933-) (sejtbiológus, molekuláris genetikus)
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9.

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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10.

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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11.

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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12.

001-es BibID:BIBFORM039004
035-os BibID:PMID:19851727
Első szerző:Penyige András (molekuláris genetikus)
Cím:Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor M145 / András Penyige, Judit Keseru, Ferenc Fazakas, Iván Schmelczer, Krisztina Szirák, György Barabás, Sándor Biró
Dátum:2009
ISSN:1225-8873
Megjegyzések:Mono-ADP-ribosylation is the enzymatic transfer of ADP-ribose from NAD(+) to acceptor proteins catalyzed by ADP-ribosyltransferases. Using m-aminophenylboronate affinity chromatography, 2D-gel electrophoresis, in-gel digestion and MALDI-TOF analysis we have identified eight in vitro ADP-ribosylated proteins in Streptomyces coelicolor, which can be classified into three categories: (i) secreted proteins; (ii) metabolic enzymes using NAD(+)/NADH or NADP(+)/NADPH as coenzymes; and (iii) other proteins. The secreted proteins could be classified into two functional categories: SCO2008 and SC05477 encode members of the family of periplasmic extracellular solute-binding proteins, and SCO6108 and SC01968 are secreted hydrolases. Dehydrogenases are encoded by SC04824 and SC04771. The other targets are GlnA (glutamine synthetase I., SC02198) and SpaA (starvation-sensing protein encoded by SC07629). SCO2008 protein and GlnA had been identified as ADP-ribosylated proteins in previous studies. With these results we provided experimental support for a previous suggestion that ADP-ribosylation may regulate membrane transport and localization of periplasmic proteins. Since ADP-ribosylation results in inactivation of the target protein, ADP-ribosylation of dehydrogenases might modulate crucial primary metabolic pathways in Streptomyces. Several of the proteins identified here could provide a strong connection between protein ADP-ribosylation and the regulation of morphological differentiation in S. coelicolor.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein ADP-ribosylation
Streptomyces coelicolor
MALDI-TOF
2-D PAGE
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal Of Microbiology. - 47 : 5 (2009), p. 549-556. -
További szerzők:Fazakas Ferenc (1969-) (molekuláris biológus) Schmelczer Iván Keserű Judit (1976-) (molekuláris genetikus) Szirák Krisztina (1973-) (molekuláris genetikus) Barabás György (1933-) (sejtbiológus, molekuláris genetikus) Biró Sándor (1949-) (molekuláris genetikus)
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