| Autor: |
Chieh-Hua Chen, Yalun Cui, Clampitt, Denae J., Burgess, Michelle E., Jenq-Kuen Huang, Wen, Lisa |
| Předmět: |
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| Zdroj: |
FASEB Journal; Apr2007, Vol. 21 Issue 6, pA1005-A1005, 1/6p |
| Abstrakt: |
The mature eukaryotic initiation factor 5A (elF5A) is the only known protein in eukaryotic cells that contains the unusual amino acid hypusine. Synthesis of hypusine is essential for the function of elF5A in eukaryotic cell proliferation and survival. Deoxyhypusine hydroxylase (DOHH), characterized as a HEAT repeat containing metalloenzyme, is the second of the two enzymes that catalyze the maturation of elF5A. DOHH has never been purified to homogeneity from any sources at the protein level. Our previous efforts in partial purification of bovine testis DOHH by a 5′ AMP affinity chromatography revealed multiple forms of DOHH. In this abstract, we report characterization of three HEAT-like repeat containing cDNA clones derived from bovine brain. Two of the clones are 912 bp in length and encodes a protein of 303 amino acid residues. The two deduced proteins differ in one amino acid substitution. The substitution resulted in reduction of DOHH activity in catalyzing the hydroxylation of the deoxyhypusine residue in the eIF5A intermediate. The third clone is 657 bp in length and encodes a protein of 218 amino acid residues. Protein alignment showed deletion of N-terminal HEAT repeat which resulted in diminished DOHH activity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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