Purification and characterization of human deoxyhypusine synthase from HeLa cells.
Post-translational modification of a specific lysine residue in eukaryotic initiation factor 5A is essential for cell viability. The amino acid hypusine, which is the product of this modification, is derived in two subsequent enzyme-catalyzed reactions. We have purified and characterized the enzyme responsible for the first step in hypusine modification, deoxyhypusine synthase, from HeLa cells. The human enzyme is multimeric with a native apparent molecular weight of 150,000 consisting of subunits of 41,000. The amino acid sequences of its peptide fragments share high sequence identity with a hypothetical protein (YHRO68w) on chromosome VIII of Saccharomyces cerevisiae. This protein appears to be the deoxyhypusine synthase of yeast.
Klier
H
H
SANDOZ Research Institute, Vienna, Austria.
Csonga
R
R
Steinkasserer
A
A
Wöhl
T
T
Lottspeich
F
F
Eder
J
J
D000595:Amino Acid Sequence; D002874:Chromosome Mapping; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D010448:Peptide Initiation Factors / Q000378:metabolism; D011487:Protein Conformation; D016601:RNA-Binding Proteins; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D000097574:Eukaryotic Translation Initiation Factor 5A
D000587:Oxidoreductases Acting on CH-NH Group Donors; D010448:Peptide Initiation Factors; D016601:RNA-Binding Proteins; D000097574:Eukaryotic Translation Initiation Factor 5A; C063507:deoxyhypusine synthase