Autor: |
Grachev, Mikhail A., Mustaev, Arkadij A., Zaychikov, Evgeny F., Lindner, Anton J., Hartmann, Guido R. |
Zdroj: |
FEBS Letters; January 1989, Vol. 250 Issue: 2 p317-322, 6p |
Abstrakt: |
RNA polymerase from the archaebacterium Sulfolobus acidocaldariuswas chemically modified with AMP o-formylphenyl ester followed by reduction with borohydride. The modified protein catalyzes the labeling of its own largest subunit when incubated with [α- 33P]UTP in the presence of poly[d(A-T)]. On cleaving of the labeled protein using cyanogen bromide, hydroxylamine or amino acid-specific endoproteinases for a very brief period, the pattern and size of the radioactive fragments formed are best explained by attachment of the label between Gly 843and Met 895of the largest subunit. In this region there exists a highly conserved sequence which is also found in other archaebacterial, eukaryotic and prokaryotic RNA polymerases. This suggests that the binding site for the initiating substrate of RNA polymerases has been conserved during evolution. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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