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J. Biol. Chem., Vol. 277, Issue 35, 31303-31309, August 30, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/35/31303    most recent M204052200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Canonaco, F. Articles by Sauer, U. Search for Related Content PubMed PubMed Citation Articles by Canonaco, F. Articles by Sauer, U. Social Bookmarking                      What's this?

Functional Expression of Phosphagen Kinase Systems Confers Resistance to Transient Stresses in Saccharomyces cerevisiae by Buffering the ATP Pool^*

Fabrizio Canonaco, Uwe Schlattner^§, Pamela S. Pruett^¶, Theo Wallimann^§, and Uwe Sauer

From the Institutes of  Biotechnology and ^§ Cell Biology, Eidgenössiche Technische Hochschule Zürich, CH-8093 Zürich, Switzerland and the ^¶ Kasha Laboratory of Biophysics, Florida State University, Tallahassee, Florida 32306-4380

Phosphagen kinase systems provide different advantages to tissues with high and fluctuating energy demands, in particular an efficient energy buffering system. In this study we show for the first time functional expression of two phosphagen kinase systems in Saccharomyces cerevisiae, which does not normally contain such systems. First, to establish the creatine kinase system, in addition to overexpressing creatine kinase isoenzymes, we had to install the biosynthesis pathway of creatine by co-overexpression of L-arginine:glycine amidinotransferase and guanidinoacetate methyltransferase. Although we could achieve considerable creatine kinase activity, together with more than 3 mM intracellular creatine, this was not sufficient to confer an obvious advantage to the yeast under the specific stress conditions examined here. Second, using arginine kinase, we successfully installed an intracellular phosphagen pool of about 5 mM phosphoarginine. Such arginine kinase-expressing yeast showed improved resistance under two stress challenges that drain cellular energy, which were transient pH reduction and starvation. Although transient starvation led to 50% reduced intracellular ATP concentrations in wild-type yeast, arginine kinase overexpression stabilized the ATP pool at the pre-stress level. Thus, our results demonstrate that temporal energy buffering is an intrinsic property of phosphagen kinases that can be transferred to phylogenetically very distant organisms.

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