Összesen 2 találat.


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: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
Rekordok letöltése1