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One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers
Author(s) -
Conrad Christian,
Schmitt Jens Guido,
Evguenieva-Hackenberg Elena,
Klug Gabriele
Publication year - 2002
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/s0014-5793(02)02653-4
Subject(s) - endoribonuclease , protein subunit , escherichia coli , cleavage (geology) , mutant , chemistry , substrate (aquarium) , biochemistry , enzyme , stereochemistry , substrate specificity , biology , rna , gene , paleontology , ecology , fracture (geology) , rnase p
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 substrate binding of a rnc70 ‐homodimer. Our results show that one functional active site is sufficient for cleavage activity of the heterodimer.