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- Title
RimJ is responsible for N<sup>α</sup>-acetylation of thymosin α1 in Escherichia coli.
- Authors
Hongqing Fang; Xu Zhang; Lin Shen; Xinxi Si; Yuantao Ren; Hongmei Dai; Shulong Li; Changlin Zhou; Huipeng Chen
- Abstract
Nα-Acetylation is one of the most common protein modifications in eukaryotes but a rare event in prokaryotes. Some endogenously Nα-acetylated proteins in eukaryotes are frequently reported not to be acetylated or only very partially when expressed in recombinant Escherichia coli. Thymosin α1 (Tα1), an Nα-acetylated peptide of 28 amino acids, displays a powerful general immunostimulating activity. Here, we revealed that a fusion protein of thymosin α1 and L12 is partly Nα-acetylated in E. coli. Through deletion of some Nα-acetyltransferases by Red recombination, we found that, when rimJ is disrupted, the fusion protein is completely unacetylated. The relationship of rimJ and Nα-acetylation of Tα1 was further investigated by gene rescue and in vitro modification. Our results demonstrate that Nα-acetylation of recombinant Tα1-fused protein in E. coli is catalyzed by RimJ and that fully acetylated Tα1 can be obtained by co-expressing with RimJ. This is the first description that an ectopic protein acetylation in bacterial expression systems is catalyzed by RimJ, a known prokaryotic Nα-acetyltransferase.
- Publication
Applied Microbiology & Biotechnology, 2009, Vol 84, Issue 1, p99
- ISSN
0175-7598
- Publication type
Academic Journal
- DOI
10.1007/s00253-009-1994-8