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Papers In Press, published online ahead of print January 22, 2002
Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107
Corresponding Author: brenner{at}dada.jci.tju.edu
The histidine triad superfamily of nucleotide hydrolases and nucleotide transferases consists of a branch of proteins related to Hint and Aprataxin, a branch of Fhit-related hydrolases, and a branch of GalT-related transferases. While substrates of Fhit and GalT are known and consequences of mutations in Aprataxin, Fhit and GalT are known, good substrates had not been reported for any member of the Hint branch and mutational consequences were unknown for Hint orthologs, which are the most ancient and widespread proteins in the Hint branch and in the histidine triad superfamily. Here we show that rabbit and yeast Hint hydrolyze the natural product adenosine-5'- monophosphoramidate in an active-site dependent manner at second order rates exceeding 1,000,000 M-1 s-1. Yeast strains constructed with specific loss of the Hnt1 active site fail to grow on galactose at elevated temperature. Loss of Hnt1 enzyme activity also leads to hypersensitivity to mutations in Ccl1, Tfb3 and Kin28, which constitute the TFIIK kinase subcomplex of general transcription factor TFIIH, and to mutations in Cak1, which phosphorylates Kin28. The target of Hnt1 regulation in this pathway was shown to be downstream of Cak1 and not to affect stability of Kin28 monomers. Functional complementation of all Hnt1 phenotypes was provided by rabbit Hint, which is only 22% identical to yeast Hnt1 but has very similar adenosine monophosphoramidase activity.
J. Biol. Chem, 10.1074/jbc.M111480200
Submitted on December 2, 2001
Revised on January 14, 2002
Accepted on January 18, 2002
Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1 and Tfb3
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