Overexpression of bacterial hemoglobin causes incorporation of pre-beta-lactamase into cytoplasmic inclusion bodies.
The expression of Vitreoscilla hemoglobin (VHb) in Escherichia coli JM101 (pRED2) causes the incorporation of the TEM beta-lactamase precursor into cytoplasmic inclusion bodies (IBs). Less pre-beta-lactamase is translocated and processed to its mature, periplasmic form in the strain coexpressing VHb than in the control strain E. coli JM101(pUC19) not expressing VHb. When cells are grown in a special fed-batch procedure, the formation of cytoplasmic IBs consisting of pre-beta-lactamase is also inducible in the control strain. Comparative microscopic and compositional analyses of IBs generated in E. coli JM101(pUC19) and JM101(pRED2) under identical growth conditions strongly suggest that pre-beta-lactamase and VHb coaggregate into common IBs in E. coli JM101 (pRED2).
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
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Rinas
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Bailey
D004926:Escherichia coli / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006454:Hemoglobins / Q000235:genetics*; D002479:Inclusion Bodies / Q000378:metabolism* / Q000648:ultrastructure; D008854:Microscopy, Electron; D014178:Translocation, Genetic; D001618:beta-Lactamases / Q000378:metabolism*
D006454:Hemoglobins; C055184:beta-lactamase TEM-3; D001618:beta-Lactamases