2011Letters in BiotechnologyRequires access

Effect of N~α-Terminal Acetyltransferase RimI on Human Prothymosin α Acetylation Expressed in Escherichia coli

Chang Shao

Open publisher page 0 citations

Abstract

Objective:To investigate the effect of RimI,one of the Nα-terminal acetyltransferases of E.coli,on human prothymosin α(ProTα) acetylation.Methods:The human ProTα and Nα-terminal acetyltransferase RimI were co-expressed in E.coli DH5α.To observe the level of N-terminal acetylation on human ProTα,ProTα was purified and detected by HPLC.Results:The ProTα was post-translational acetylated.Over-expression of RimI,long term induction and the cross-effect could affect the level of N-terminal acetylation of ProTα(P0.0001).The increasing N-terminal acetylated ProTα could be observed after inducing 6 h,whether RimI was over-expressed or not(P0.0001).There were 37.4% N-terminal acetylated ProTα in the presence of overdose RimI,64.3% N-terminal acetylated ProTα without of overdose RimI after inducing 12 h,and we could observe the inhibition after inducing 6 h(P=0.0007).Conclusion:The N-terminal acetylation of ProTα was inhibited when over-expressed Nα-terminal acetyltransferase RimI.

About this research paper

What this paper is about

Objective:To investigate the effect of RimI,one of the Nα-terminal acetyltransferases of E.coli,on human prothymosin α(ProTα) acetylation.Methods:The human ProTα and Nα-terminal acetyltransferase RimI were co-expressed in E.coli DH5α.To observe the level of N-terminal acetylation on human ProTα,ProTα was purified and detected by HPLC.Results:The ProTα was post-translational acetylated.Over-expression of RimI,long term induction and the cross-effect could affect the level of N-terminal acetylation of ProTα(P0.0001).The increasing N-terminal acetylated ProTα could be observed after inducing 6 h,whether RimI was over-expressed or not(P0.0001).There were 37.4% N-terminal acetylated ProTα in the presence of overdose RimI,64.3% N-terminal acetylated ProTα without of overdose RimI after inducing 12 h,and we could observe the inhibition after inducing 6 h(P=0.0007).Conclusion:The N-terminal acetylation of ProTα was inhibited when over-expressed Nα-terminal acetyltransferase RimI.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Objective:To investigate the effect of RimI,one of the Nα-terminal acetyltransferases of E.coli,on human prothymosin α(ProTα) acetylation.Methods:The human ProTα and Nα-terminal acetyltransferase RimI were co-expressed in E.coli DH5α.To observe the level of N-terminal acetylation on human ProTα,ProTα was purified and detected by HPLC.Results:The ProTα was post-translational acetylated.Over-expression of RimI,long term induction and the cross-effect could affect the level of N-terminal acetylation of ProTα(P0.0001).The increasing N-terminal acetylated ProTα could be observed after inducing 6 h,whether RimI was over-expressed or not(P0.0001).There were 37.4% N-terminal acetylated ProTα in the presence of overdose RimI,64.3% N-terminal acetylated ProTα without of overdose RimI after inducing 12 h,and we could observe the inhibition after inducing 6 h(P=0.0007).Conclusion:The N-terminal acetylation of ProTα was inhibited when over-expressed Nα-terminal acetyltransferase RimI.

Key concepts: Acetylation, Acetyltransferase, Acetyltransferases, Escherichia coli, N-acetyltransferase, Biochemistry, Acetyl-CoA, Terminal (telecommunication)

Related papers

Back to paper searchBrowse research topicsOriginal source
Effect of N~α-Terminal Acetyltransferase RimI on Human Prothymosin α Acetylation Expressed in Escherichia coli — Research Paper | ScholarLens