Article
Aggregation of heat-shock-denatured, endogenous proteins and distribution of the IbpA/B and Fda marker-proteins in Escherichia coli WT and grpE280 cells.
Microbiology (Reading, England) - 1 Jan 2004
Laskowska Ewa, Bohdanowicz Jerzy, Kuczyńska-Wiśnik Dorota, Matuszewska Ewelina, Kędzierska Sabina, Taylor Alina
Abstract excerpt
Submission of wild-type Escherichia coli to heat shock causes an aggregation of cellular proteins. The aggregates (S fraction) are separable from membrane fractions by ultracentrifugation in a sucrose density gradient. In contrast, no protein aggregation was detectable in an E. coli grpE280 mutant either by this technique or by electron microscopy. In search of an explanation for this observation at a molecular...
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