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001-es BibID:BIBFORM009630
Első szerző:Hádáné Birkó Zsuzsanna (molekuláris genetikus)
Cím:Lack of A-factor production induces the expression of nutrient scavenging and stress-related proteins in Streptomyces griseus / Birkó Zsuzsanna, Swiatek Magdalena, Szájli Emília, Medzihradszky F. Katalin, Vijgenboom Erik, Penyige András, Keserű Judit, van Wezel Gilles P., Biró Sándor
Dátum:2009
ISSN:1535-9476 (Print)
Megjegyzések:The small gamma-butyrolactone A-factor is an important autoregulatory signaling molecule for the soil-inhabiting streptomycetes. Starvation is a major trigger for development,and nutrients are provided by degradation of the vegetative mycelium via a process of programmed cell death, reusing proteins, nucleic acids, and cell wall material. The A-factor regulon includes many extracellular hydrolases. Here we show via proteomics analysis that many nutrientscavenging and stress-related proteins were overexpressed in an A-factor non-producing mutant of Streptomyces griseus B-2682. Transcript analysis showed that this is primarily due to differential transcription of the target genes during early development. The targets include proteins relating to nutrient stress and environmental stress and an orthologue of the Bacillus sporulation control protein Spo0M. The enhanced expression of these proteins underlines the stress that is generated by the absence of A-factor. Wild-type developmental gene expression was restored to the A-factor non-producing mutant by the signaling protein Factor C in line with our earlier observation that Factor C triggers A-factor production.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
C-faktor
Streptomyces griseus
proteomika
Megjelenés:Molecular and Cellular Proteomics : MCP - 8 : 10 (2009), p. 2396-2403. -
További szerzők:Swiatek, Magdalena Szájli Emília Medzihradszky-Fölkl Katalin Vijgenboom, Erik Penyige András (1954-) (molekuláris genetikus) Keserű Judit (1976-) (molekuláris genetikus) Wezel, Gilles P., van Biró Sándor (1949-) (molekuláris genetikus)
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2.

001-es BibID:BIBFORM028739
Első szerző:Keserű Judit (molekuláris genetikus)
Cím:Identification of beta-lactamases in human and bovine isolates of Staphylococcus aureus strains having borderline resistance to penicillinase-resistant penicillins (PRPs) with proteomic methods / Keserű Judit Szilvia, Szabó István, Gál Zsuzsanna, Orietta Massidda, Marina Mingoia, Kaszanyitzky Éva, Jánosi Szilárd, Hulvely Julianna, Csorba Attila, Buzás Krisztina, Hunyadi-Gulyás Éva, Medzihradszky F. Katalin, Biró Sándor
Dátum:2011
ISSN:0378-1135
Megjegyzések:Methicillin and oxacillin-hydrolyzing enzymes of 6 borderline methicillin-resistant and 1 methicillin-resistant Staphylococcus aureus strains isolated from human clinical samples and 4 borderline methicillin-resistant S. aureus strains isolated from bovine mastitis were investigated. As previous studies suggested the involvement of an additional enzyme besides the penicillinase BlaZ in the determination of borderline resistance, we analyzed the expressed extracellular and membrane-bound beta-lactamases with 2-D gel electrophoresisand mass spectrometry. Our analysis showed that the penicillin-hydrolyzing BlaZ alone was responsible for the hydrolysis of both methicillin and oxacillin. All supernatant and membrane fractions contained the same enzyme with slight sequence variations. The size and pI of the proteins were also variable, probably due to spontaneous hydrolysis and/or posttranslational modifications. Interestingly, we found also cytotoxins and other virulence factors in some nitrocefin-hydrolyzing dots, suggesting that those proteins might have a role in the reduction of local antibiotic concentration.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Staphylococcus aureus
Borderline methicillin-resistance
Membrane-bound beta-lactamase
Penicillinase
PRPs-hydrolyzing enzyme
Proteomics
Megjelenés:Veterinary Microbiology. - 147 : 1-2 (2011), p. 96-102. -
További szerzők:Szabó István (1950-) (sejtbiológus, molekuláris genetikus) Gál Zsuzsanna (1959-) (vegyész) Massidda, Orietta Mingoia, Marina Kaszanyitzky J. Éva Jánosi Szilárd Hulvely Julianna Csorba Attila Buzás Krisztina Hunyadi-Gulyás Éva Medzihradszky-Fölkl Katalin Biró Sándor (1949-) (molekuláris genetikus)
Pályázati támogatás:ETT 395/KO/03
Egyéb
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DOI
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3.

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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4.

001-es BibID:BIBFORM039003
035-os BibID:PMID:22752904
Első szerző:Szirák Krisztina (molekuláris genetikus)
Cím:Disruption of SCO5461 gene coding for a mono-ADP-ribosyltransferase enzyme produces a conditional pleiotropic phenotype affecting morphological differentiation and antibiotic production in Streptomyces coelicolor / Krisztina Szirák, Judit Keserű, Sándor Biró, Iván Schmelczer, György Barabás, András Penyige
Dátum:2012
ISSN:1225-8873
Megjegyzések:The SCO5461 gene of Streptomyces coelicolor A3(2) codes for an ADP-ribosyltransferase enzyme that is predicted to be a transmembrane protein with an extracellular catalytic domain. PCR-targeted disruption of the gene resulted in a mutant that differentiated normally on complex SFM medium; however, morphological differentiation in minimal medium was significantly delayed and this phenotype was even more pronounced on osmotically enhanced minimal medium. The mutant did not sporulate when it was grown on R5 medium, however the normal morphological differentiation was restored when the strain was cultivated beside the wild-type S. coelicolor M145 strain. Comparison of the pattern of ADP-ribosylated proteins showed a difference between the mutant and the wild type, fewer modified proteins were present in the cellular crude extract of the mutant strain. These results support our previous suggestions that protein ADP-ribosylation is involved in the regulation of differentiation and antibiotic production and secretion in Streptomyces.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Streptomyces
egyetemen (Magyarországon) készült közlemény
mono-ADP-ribosyltransferase
protein ADP-ribosylation
morphological differentiation
actinorhodin production and secretion
Megjelenés:Journal of Microbiology. - 50 : 3 (2012), p. 409-418. -
További szerzők:Schmelczer Iván Keserű Judit (1976-) (molekuláris genetikus) Biró Sándor (1949-) (molekuláris genetikus) Barabás György (1933-) (sejtbiológus, molekuláris genetikus) Penyige András (1954-) (molekuláris genetikus)
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