Cellular localization of the Escherichia coli SpoT protein

Author:

Gentry D R1,Cashel M1

Affiliation:

1. Section on Molecular Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.

Abstract

The SpoT protein of Escherichia coli serves as a source of degradation as well as an apparent source of synthesis of (p)ppGpp. Since the subcellular localization of SpoT might be a clue to its function, we have used SpoT-specific antisera to analyze cell extracts fractionated on sucrose gradients. We find that the SpoT protein is not bound to ribosomes or to either inner or outer membrane fractions. Although the SpoT protein is found in large aggregates, its localization is probably cytosolic.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference31 articles.

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2. Cashel M. and K. E. Rudd. 1987. The stringent response p. 1410-1438. In F. C. Neidhardt J. L. Ingraham K. B. Low B. Magasanik M. Shaechter and H. E. Umbarger (ed.) Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology Washington D.C.

3. On the turnover of ppGpp in Escherichia coli;Gallant J.;J. Biol. Chem.,1972

4. Gentry D. R. and M. Cashel. Unpublished data.

5. Synthesis of the stationary-phase specific sigma factor, ~s, is positively regulated by ppGpp;Gentry D. R.;J. Bacteriol.,1993

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