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PMID: 7601859 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Cellular localization of the Escherichia coli SpoT protein.

Journal of bacteriology ·Vol. 177 ·No. 13 ·1995-07-00 ·Pages 3890-3

Gentry DR, Cashel M

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.

MeSH Terms
Cell Compartmentation Cell Fractionation Cytosol Escherichia coli/physiology Membranes/chemistry Pyrophosphatases/isolation & purification
Chemicals
guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase Pyrophosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gentry D R
Section on Molecular Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
Cashel M
References (27)
27 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.177.13.3890-3893.1995
Published
1995-07-00
Pages
3890-3
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC177113
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.177.13.3890-3893.1995 PMC Full Text View journal details
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