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Appl Microbiol Biotechnol. 2009 Aug;84(1):99-104. doi: 10.1007/s00253-009-1994-8. Epub 2009 Apr 8.

RimJ is responsible for N(alpha)-acetylation of thymosin alpha1 in Escherichia coli.

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  • 1Institute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, People's Republic of China. fanghongqing@vip.sina.com


N(alpha)-Acetylation is one of the most common protein modifications in eukaryotes but a rare event in prokaryotes. Some endogenously N(alpha)-acetylated proteins in eukaryotes are frequently reported not to be acetylated or only very partially when expressed in recombinant Escherichia coli. Thymosin alpha1 (Talpha1), an N(alpha)-acetylated peptide of 28 amino acids, displays a powerful general immunostimulating activity. Here, we revealed that a fusion protein of thymosin alpha1 and L12 is partly N(alpha)-acetylated in E. coli. Through deletion of some N(alpha)-acetyltransferases by Red recombination, we found that, when rimJ is disrupted, the fusion protein is completely unacetylated. The relationship of rimJ and N(alpha)-acetylation of Talpha1 was further investigated by gene rescue and in vitro modification. Our results demonstrate that N(alpha)-acetylation of recombinant Talpha1-fused protein in E. coli is catalyzed by RimJ and that fully acetylated Talpha1 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 N(alpha)-acetyltransferase.

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