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  • 1
    Electronic Resource
    Electronic Resource
    A transcription factor IIB homolog from the hyperthermophilic archaeon Pyrococcus furiosus binds Zn or Fe in an N-terminal Cys4 motif (1996)
    Springer
    JBIC 1 (1996), S. 162-168 
    Details
    ISSN: 1432-1327
    Keywords: Key words TFIIB ; Metalloprotein ; Zinc finger ; Gene transcription ; X-ray absorption spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The gene for an archaeal homolog of the eukaryotic transcription factor TFIIB has been cloned from the marine hyperthermophilic archaeon Pyrococcus furiosus and overexpressed in Escherichia coli. This TFB gene displays a sequence that is identical to a gene sequence in P. woesei. A gene for the 49-residue N-terminal domain of TFB that contains a putative C-X2-C-X15-C-X2-C metal-binding motif was subcloned and overexpressed as TFB-NTD. Purification of the TFB-NTD gene product yields Zn- and Fe-containing forms, which have been characterized by mass spectrometry and UV-visible, electron paramagnetic resonance, and X-ray absorption (XAS) spectroscopies. Only the Zn form of the TFB holoprotein has been (partially) purified, and it has been characterized by XAS. All spectroscopic characteristics are consistent with a nearly tetrahedral MS4 metal-binding site made up of the four cysteine residues in the N-terminal domain. The relatively greater thermal stability of the Zn form suggests that TFB may be a Zn-containing protein involved in archaeal transcription.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050035
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  • 2
    Electronic Resource
    Electronic Resource
    Structural evidence for a common zinc binding domain in archaeal and eukaryal transcription factor IIB proteins (2000)
    Springer
    JBIC 5 (2000), S. 276-283 
    Details
    ISSN: 1432-1327
    Keywords: Key words Transcription factor IIB ; Metalloprotein ; Zinc finger ; Gene transcription ; X-ray absorption spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract X-ray absorption spectroscopy has been used to compare the metal coordination of the N-terminal zinc binding domain of eukaryal human transcription factor (TF) IIB to the previously reported structure of archaeal Pyrococcus furiosus (Pf) TFB. Full length and N-terminal fragments for both PfTFBand human TFIIB were cloned, expressed, and purified. The [C10H] variant of PfTFB was constructed to resemble the metal binding motif of higher eukaryal TFIIB proteins by mutating the second cysteine ligand to a histidine. All five proteins bind zinc in a 1 :1 ratio. Zn X-ray absorption spectroscopy of human TFIIB and [C10H]PfTFB mutant are consistent with ZnS3(N,O) ligation, and further suggest that the N/O ligand is an imidazole.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050372
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