期刊
BIOCHEMICAL JOURNAL
卷 433, 期 -, 页码 205-213出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20101322
关键词
acetylation; eukaryotic translation initiation factor 5A (eIF5A); hypusine; polyamine metabolism; post-translational modification; spermidine/spermine-N(1-)acetyltransferase 1 (SSAT1)
资金
- National Institute of Dental and Craniofacial Research (NIDCR)
- National Institute of Drug Abuse (NIDA)
- National Institute on Alcohol Abuse and Alcoholism (NIAA)
- National Institutes of Health (NIH) [R01 GM092927]
- Human Frontier Science Program fellowship [LT00575/2007-L]
- NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH [ZIADE000608] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM092927] Funding Source: NIH RePORTER
eIF5A (eukaryotic translation initiation factor 5A) is the only cellular protein containing hypusine [N-epsilon-(4-amino-2-hydroxybutyl)lysine]. eIF5A is activated by the post-translational synthesis of hypusine and the hypusine modification is essential for cell proliferation. In the present study, we report selective acetylation of the hypusine and/or deoxyhypusine residue of eIF5A by a key polyamine catabolic enzyme SSAT1 (spermidine/spermine-N-1-acetyltransferase 1). This enzyme normally catalyses the N-1 -acetylation of spermine and spermidine to form acetyl-derivatives, which in turn are degraded to lower polyamines. Although SSAT1 has been reported to exert other effects in cells by its interaction with other cellular proteins, eIF5A is the first target protein specifically acetylated by SSAT1. Hypusine or deoxyhypusine, as the free amino acid, does not act as a substrate for SSAT1, suggesting a macromolecular interaction between eIF5A and SSAT1. Indeed, the binding of eIF5A and SSAT1 was confirmed by pull-down assays. The effect of the acetylation of hypusine on eIF5A activity was assessed by comparison of acetylated with non-acetylated bovine testis eIF5A in the methionyl-puromycin synthesis assay. The loss of eIF5A activity by this SSAT1-mediated acetylation confirms the strict structural requirement for the hypusine side chain and suggests a possible regulation of eIF5A by hypusine acetylation/deacetylation.
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