Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli.
The protein composition of inclusion bodies produced in recombinant Escherichia coli overproducing Vitreoscilla hemoglobin (VHb) was analyzed by one-dimensional and two-dimensional electrophoresis techniques. Results indicate the presence of two types of cytoplasmic aggregates of differing morphology in single bacterial cells. These aggregates also differ in their relative content of VHb and pre-beta-lactamase and are separable by differential centrifugation. Results further suggest that the cytoplasmic protein elongation factor Tu is integrated into VHb inclusion bodies. The presence of the outer membrane proteins OmpA and OmpF in inclusion body preparations is attributed to cell envelope contamination rather than specific involvement in inclusion bodies. The specificity of in vivo protein aggregation is discussed.
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
R A
RA
Hart
U
U
Rinas
J E
JE
Bailey
D000818:Animals; D001419:Bacteria / Q000378:metabolism*; D015153:Blotting, Western; D004220:Disulfides; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism* / Q000648:ultrastructure; D006454:Hemoglobins / Q000378:metabolism* / Q000648:ultrastructure; D010957:Plasmids; D011485:Protein Binding; D011994:Recombinant Proteins / Q000648:ultrastructure*; D012995:Solubility; D001618:beta-Lactamases / Q000235:genetics
D004220:Disulfides; D006454:Hemoglobins; D011994:Recombinant Proteins; D001618:beta-Lactamases