BB-kb@ldeleger:BB-kb-9535771 JSON TXT

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Id	Subject	Object	Predicate	Lexical cue	NCBI_Taxonomy	OntoBiotope
T1	0-103	Title	denotes	Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli.
T3	39-48	Habitat	denotes	mammalian		OBT:001625
T4	86-102	Microorganism	denotes	Escherichia coli	562
T2	104-1049	Paragraph	denotes	We made fusions between Escherichia coli maltose-binding protein (MBP) and the mammalian aspartic proteinases pepsinogen or procathepsin D. When MBP was at the N-terminus, the fusions were soluble in E. coli. When the order was reversed, the chimeric proteins formed inclusion bodies. The data suggest that the solubility of fusion proteins is controlled by whether the protein domains emerging first from the ribosome normally fold into soluble or insoluble states. The soluble MBP-aspartic proteinase fusions were stable but proteolytically inactive. MBP-pepsinogen, however, was efficiently renatured from 8 M urea in vitro, suggesting that the E. coli cytoplasm does not support folding of the mammalian partner protein to the native state. Thus, inclusion body formation may be the consequence, rather than the cause, of non-native folding in vivo, and in E. coli soluble proteins may fold into states different from those reached in vitro.
T5	128-144	Microorganism	denotes	Escherichia coli	562
T6	183-192	Habitat	denotes	mammalian		OBT:001625
T7	304-311	Microorganism	denotes	E. coli	562
T8	752-759	Microorganism	denotes	E. coli	562
T9	802-811	Habitat	denotes	mammalian		OBT:001625
T10	965-972	Microorganism	denotes	E. coli	562