Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase

Lei Xiao, Paul Celano, Amy R. Mank, Anthony E. Pegg, Robert A. Casero

Research output: Contribution to journalArticle

Abstract

Spermidine/spermine N1-acetyltransferase is the rate-limiting enzyme in the catabolism of cellular polyamines. Using a combination of cDNA library screening and anchored PCR methodologies, a full length cDNA designated AP3 F7 corresponding to the human SSAT was cloned using RNA from the human large cell undifferentiated lung carcinoma line NCI H157. The resulting cDNA clone is 1,060 base pairs with a 513 base open reading frame coding for a 171 amino acid protein, with a predicted subunit molecular weight of 20,023. The 5′ non-coding region of AP3 F7 is 165 bases and the 3′ untranslated region is 382 bases with a polyadenylation site 20 bases 5′ to the poly(A) tail. This full length cDNA should be an aid in the study of the regulation of spermidine/spermine N1-acetyltransferase expression and the significance of the acetyltransferase in polyamine metabolism.

Original languageEnglish (US)
Pages (from-to)407-415
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume179
Issue number1
DOIs
StatePublished - Aug 30 1991

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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