Acetyl Phosphate as an Energy Source for Bacterial Cell-Free Translation Systems

Ryabova, Lyubov A.; Vinokurov, Leonid M.; Shekhovtsova, E. A.; Alakhov, Yu.B.; Spirin, Alexander S.

doi:10.1006/abio.1995.1208

Cited by 67 publications

(33 citation statements)

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“…Some organisms are able to condense pyruvate with inorganic phosphate to produce acetyl phosphate using pyruvate oxidase (EC 1.2.3.3) (Muller et al, 1993). Because acetyl phosphate can be used as an energy source for protein synthesis (Ryabova et al, 1995), the pyruvate oxidase reaction provides the basis for a new scheme to regenerate ATP that has been hydrolyzed in the process of protein synthesis (see Fig. 1B).…”

Section: Introductionmentioning

confidence: 99%

Prolonging cell-free protein synthesis with a novel ATP regeneration system

Kim¹,

Swartz²

1999

Biotechnol. Bioeng.

215

149

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Section: Introductionmentioning

confidence: 99%

Prolonging cell-free protein synthesis with a novel ATP regeneration system

Kim¹,

Swartz²

1999

Biotechnol. Bioeng.

215

149

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“…Transcription Reactions. Coupled transcription/translation was accomplished by adding ribosomes to ribosome-free translation extracts prepared from strain SM1200 (SM1090, S10::kan supported by pS10 encoding L22 with a FLAG epitope) and was based on published protocols (32)(33)(34). A template plasmid from which mRNAs for SspB and ␤-lactamase are transcribed from a T7 promoter was used to direct synthesis of 14 C-labeled proteins (35) as described in SI Text.…”

Section: Methodsmentioning

confidence: 99%

Forced extraction of targeted components from complex macromolecular assemblies

Moore¹,

Baker

Sauer³

2008

Proc. Natl. Acad. Sci. U.S.A.

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When individual protein components of supramolecular complexes are required for assembly, determining whether they play additional structural or functional roles can be difficult. Removing a protein from the complex after assembly can circumvent this problem. Here, we show that an AAA؉ unfoldase/protease can extract an essential assembly protein from the ribosome. Specifically, Mg 2؉ depletion allowed ClpXP to remove an ssrA-tagged variant of ribosomal protein L22 from the 50S subunit of E. coli ribosomes without disrupting either the structural integrity or hydrodynamic properties of the modified particle. Forced extraction using AAA؉ enzymes and targeted component proteins should be broadly applicable to the study of macromolecular complexes.AAAϩ machine ͉ ClpX ͉ disassembly chaperone ͉ ribosome ͉ L22

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“…These operating parameters are often optimized in a protein -specifi c manner. Signifi cant effort has been placed in stabilizing the concentration of easily degradable amino acids [211,212] (such as arginine, cysteine, and tryptophan) and fi nding more effi cient energy sources [207,213] (e.g., by activating oxidative phosphorylation).…”

Section: Cell -Free Protein Productionmentioning

confidence: 99%