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Article

One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers.

FEBS letters - 8 May 2002

Conrad Christian, Schmitt Jens Guido, Evguenieva-Hackenberg Elena, Klug Gabriele

Abstract excerpt

To study the intersubunit communication required for the activity of the normally homodimeric enzyme endoribonuclease III of Escherichia coli we have constructed and analysed an artificial heterodimer. This heterodimer is composed of one wild-type and one catalytically inactive subunit. The inactive subunit has one amino acid exchanged (E117K, rnc70 mutant) which abolishes cleavage activity but still allows...

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PMID: 11997024
DOI: 10.1016/s0014-5793(02)02653-4

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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