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J. Biol. Chem., Vol. 277, Issue 13, 10852-10860, March 29, 2002
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From the 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 galactose-1-phosphate uridylyltransferase (GalT)-related transferases. Although 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 (AMPNH2) in an active-site-dependent
manner at second order rates exceeding 1,000,000 M
Adenosine Monophosphoramidase Activity of Hint and Hnt1
Supports Function of Kin28, Ccl1, and Tfb3*,
,¶,
,**
Structural Biology and Bioinformatics
Program, Kimmel Cancer Center, Philadelphia, Pennsylvania 19107, § Department of Biochemistry, University of Texas Health
Sciences Center, San Antonio, Texas 78229, and Institut Curie,
UMR 2027-CNRS, 91405 Orsay, France
1 s1. Yeast strains
constructed with specific loss of the Hnt1 active site fail to grow on
galactose at elevated temperatures. 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.
*
This work was supported by National Institutes of Health
Research Grant CA75954 (NCI) (to C. B.) and National Science
Foundation Grant MCB9982645 (to L. D. B.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains Table II.
¶
Present address: Wistar Institute, Philadelphia, PA 19104.
**
To whom correspondence should be addressed: Kimmel Cancer Center,
233 S. Tenth St., Rm. 826, Philadelphia, PA 19107. Tel.: 215-503-4573;
Fax: 215-923-1696; E-mail:
brenner@dada.jci.tju.edu.
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