Literature DB >> 6804229

Identification of a class of lysines within the non-specific DNA-binding site of RNA polymerase core enzyme from Escherichia coli.

A J Makoff, A D Malcolm.   

Abstract

The imido ester, methyl acetimidate, which specifically amidinates lysine residues, modifies RNA polymerase core enzyme, leading to rapid loss of activity. Calf thymus DNA partially protects the enzyme against this inactivation, an effect which disappears at high salt concentration. DNA protects 17 +/- 6 lysines from amidination at low salt concentration. The dependence of amidination on methyl acetimidate concentration is examined in the presence of DNA at high and low salt concentration. Analysis of the data suggests a class of approximately 12 lysines which are protected by DNA, consistent with the above estimate. These lysines are approximately 5--10-fold more reactive than most other available lysine residues.

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Year:  1980        PMID: 6804229     DOI: 10.1111/j.1432-1033.1980.tb06025.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  6 in total

1.  Kinetics of protein modification, and/or enzyme inactivation, reactions by an unstable modifying agent.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1987-09-15       Impact factor: 3.857

Review 2.  Kinetics of protein modification reactions.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1984-01-15       Impact factor: 3.857

3.  Properties of methyl acetimidate and its use as a protein-modifying reagent.

Authors:  A J Makoff; A D Malcolm
Journal:  Biochem J       Date:  1981-01-01       Impact factor: 3.857

4.  Kinetics of irreversible enzyme inhibition by an unstable inhibitor.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1981-11-01       Impact factor: 3.857

5.  Identification of a nucleic acid-binding region within the largest subunit of Drosophila melanogaster RNA polymerase II.

Authors:  R E Kontermann; M Kobor; E K Bautz
Journal:  Protein Sci       Date:  1993-02       Impact factor: 6.725

6.  Studies of the interaction of troponin I with proteins of the I-filament and calmodulin.

Authors:  A J Moir; M Ordidge; R J Grand; I P Trayer; S V Perry
Journal:  Biochem J       Date:  1983-02-01       Impact factor: 3.857

  6 in total

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