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001-es BibID:BIBFORM025190
Első szerző:Hádáné Birkó Zsuzsanna (molekuláris genetikus)
Cím:Characterization of the gene for factor C, an extracellular signal protein involved in morphological differentiation of Streptomyces griseus / Zsuzsanna Birkó, Andrea Sümegi, Andrea Vinnai, Gilles van Wezel, Ferenc Szeszák, Sándor Vitális, Pál T. Szabó, Zoltán Kele, Tamás Janáky, Sándor Biró
ISSN:1350-0872 1465-2080
Megjegyzések:The gene encoding factor C (facC), an extracellular signal protein involved in cellular differentiation, was cloned from Streptomyces griseus 45H, and the complete nucleotide sequence was determined. The deduced amino acid sequence was confirmed by HPLC/electrospray ionization-mass spectrometry analysis. The full-length protein consists of 324 amino acids and has a predicted molecular mass of 34,523 Da. The mature extracellular 286 amino acid protein (31,038 Da) is probably produced by cleaving off a 38 amino acid secretion signal sequence. Southern hybridization detected facC in several other Streptomyces strains, but database searches failed to identify a protein with significant homology to factor C. Expression of facC from a low-copy-number vector in S. griseus 52-1 resulted in a phenotypic effect similar to that given by exogenously added factor C protein.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Microbiology (Reading, England). - 145 : 9 (1999), p. 2245-2253. -
További szerzők:Sümegi Andrea (1969-) (biológus) Vinnai Andrea Wezel, Gilles van Szeszák Ferenc Vitális Sándor Szabó Pál T. Kele Zoltán Janáky Tamás Biró Sándor (1949-) (molekuláris genetikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat


001-es BibID:BIBFORM001540
Első szerző:Hádáné Birkó Zsuzsanna (molekuláris genetikus)
Cím:The secreted signaling protein factor C triggers the A-factor response regulon in streptomyces griseus : overlapping signaling routes / Birkó Z., Bialek S., Buzás K., Szájli E., Traag B. A., Medzihradszky K. F., Rigali S., Vijgenboom E., Penyige A., Kele Z., van Wezel G. P., Bíró S.
Megjegyzések:Members of the prokaryotic genus Streptomyces produce over 60% of all known antibiotics and a wide range of industrial enzymes. A leading theme in microbiology is which signals are received and transmitted by these organisms to trigger the onset of morphological differentiation and antibiotic production. The small -butyrolactone A-factor is an important autoregulatory signaling molecule in streptomycetes, and A-factor mutants are blocked in development and antibiotic production. In this study we showed that heterologous expression of the 324-amino acid secreted regulatory protein Factor C resulted in restoration of development and enhanced antibiotic production of an A-factor-deficient bald mutant of Streptomyces griseus, although the parental strain lacks an facC gene. Proteome analysis showed that in the facC transformant the production of several secreted proteins that belong to the A-factor regulon was restored. HPLC-MS/MS analysis indicated that this was due to restoration of A-factor production to wild-type levels in the transformant. This indicates a connection between two highly divergent types of signaling molecules and possible interplay between their regulatory networks.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Streptomyces szignalizáció
Megjelenés:Molecular and Cellular Proteomics : MCP - 6 : 7 (2007), p. 1248-1256. -
További szerzők:Bialek, Sylwia Buzás Krisztina Szájli Emília Traag, Bjorn A. Medzihradszky-Fölkl Katalin Rigali, Sebastien Vijgenboom, Erik Kele Zoltán Wezel, Gilles P., van Biró Sándor (1949-) (molekuláris genetikus) Penyige András (1954-) (molekuláris genetikus)
Internet cím:elektronikus változat
elektronikus változat


001-es BibID:bibEBI00010183
Első szerző:Szabó Pál T.
Cím:Identification of factor C protein from Streptomyces griseus by microelectrospray mass spectrometry / P. T. Szabó, Z. Kele, Zs. Birkó, F. Szeszák, S. Biró, T. Janáky
Megjegyzések:Factor C, an extracellular signal protein of cellular differentiation, was studied and significant homology was found to several zinc finger-type regulatory proteins. The complete amino acid sequence, deduced from the gene, that encodes the protein, did not support the hypothesis that this protein might be a zinc finger-type regulatory protein. However, a theoretical single nucleotide insertion in the gene can result in another similarly sized protein containing about 20 His residues, which would be responsible for the high zinc affinity of factor C. The protein sample was reduced, alkylated and then in-gel digested with trypsin. The peptide fragments were then separated by capillary chromatography and identified by microelectrospray mass spectrometry. Peaks of higher intensity were sequenced by tandem mass spectrometry. The identified peptide fragments and the measured molecular mass of factor C protein also confirmed the original sequence of protein, as there was no shift in the open reading frame.
Tárgyszavak:idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Mass Spectrometry. - 34 : 12 (1999), p. 1312-1316. -
További szerzők:Kele Zoltán Hádáné Birkó Zsuzsanna (1971-) (molekuláris genetikus) Szeszák Ferenc Biró Sándor (1949-) (molekuláris genetikus) Janáky Tamás
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat


001-es BibID:BIBFORM077294
Első szerző:Szilágyi Melinda (biológus)
Cím:Mutation in afsR Leads to A-Factor Deficiency in Streptomyces griseus B2682 / Melinda Szilágyi, Éva Márton, Dávid Lukács, Zsuzsanna Birkó, Zoltán Kele, Sándor Biró
Megjegyzések:A-factor, a γ-butyrolactone autoregulator, in Streptomyces griseus is involved in the regulation of differentiation and antibiotic production. Here we studied the S. griseus B2682-AFN (A-factor negative) bald mutant that harbors a nonsense mutation in the afsR gene encoding a pleiotropic regulator. Our aim was to prove that this mutation is the cause of the A-factor deficiency in AFN. We also studied whether AfsR regulates A-factor production by AfsA, which is supposed to be the only specific key enzyme in A-factor biosynthesis. METHODS: Wild afsR was cloned to the pHJL401 shuttle vector and was transformed to the S. griseus AFN and B2682 strains. During phenotypic characterization, sporulation, antibiotic, protease, A-factor, and AfsA protein production were studied. RESULTS: Transformation of AFN by a wild afsR restored its phenotype including sporulation, antibiotic, extracellular protease, and A-factor production. Introduction of afsR to the B2682 wild-type strain resulted in antibiotic and extracellular protease overproduction that was accompanied with an elevated A-factor level. AfsA was detected both in AFN and B2682. CONCLUSIONS: AfsR has an effect on the regulation of A-factor production in S. griseus. The presence of AfsA is not sufficient for normal A-factor production. AfsR regulates A-factor biosynthesis independently of AfsA.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Molecular Microbiology And Biotechnology. - 28 : 5 (2018), p. 216-224. -
További szerzők:Márton Éva (1992-) (biológus) Lukács Dávid Hádáné Birkó Zsuzsanna (1971-) (molekuláris genetikus) Kele Zoltán Biró Sándor (1949-) (molekuláris genetikus)
Internet cím:Szerző által megadott URL
Intézményi repozitóriumban (DEA) tárolt változat
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