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Cyclic adenosine‐5′‐trimetaphosphate phosphorylates a histidine residue nearby the initiating substrate binding site of Escherichia coli DNA‐dependent RNA‐polymerase
Author(s) -
Grachev M.A.,
Mustaev A.A.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80321-9
Subject(s) - dna , chemistry , escherichia coli , chinese academy of sciences , rna polymerase , dna polymerase , citation , library science , physics , biochemistry , computer science , geography , gene , china , archaeology
in the presence of a promoter template acts as an efficient affinity reagent towards the center of initiating substrate binding of DNA-dependent RNApolymerase of Escherichia coli. It was found that ATMP inactivates RNA-polymerase, the enzyme being protected from inactivation by ATP. On the contrary, addition of [w~‘P]UTP causes acceleration of the inactivation by a factor of 10-20. Radioactivity of [Q-~‘P] UTP under these conditions is bound covalently by the /3-subunit of the enzyme. These data suggested that the result of the affinity modification was phosphorylation of an ammo acid residue by an oligonucleotide synthesized by RNA-polymerase from ATMP and [a-32P]UTP. The present studies was aimed at the determination of the length of this covalently-bound oligonucleotide and at elucidation of the nature of the phosphorylated amino acid residue.