Rapidly degrading GFP-fusion proteins and methods of use

Details Rapidly degrading GFP-fusion proteins and methods of use Rapidly degrading GFP-fusion proteins and methods of use

2005-10-18

2005-10-18

Horlick, Kenneth R. (Department: 1637)

Organic compounds -- part of the class 532-570 series

Organic compounds

Carbohydrates or derivatives

C435S320100, C435S325000, C435S069100, C435S006120, C536S025300, C536S025320, C530S350000

Reexamination Certificate

active

06956112

ABSTRACT:
Green fluorescent protein (GFP) is widely used as a reporter in determining gene expression and protein localization. The present invention provides fusion proteins with a half life of ten hours or less with several embodiments having half lives of 4 hours or less. Such proteins may be constructed by fusing C-terminal amino acids of the degradation domain of mouse ornithine decarboxylase (MODC), which contains a PEST sequence, to the C-terminal end of an enhanced variant of GFP (EGFP). Fluorescence intensity of the fusion protein in transfected cells is similar to that of EGFP, but the fusion protein, unlike EGFP, is unstable in the presence of cycloheximide. Specific mutations in the MODC region have resulted in mutants with varying half lives, useful for a variety of purposes.

REFERENCES:
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INVITROGEN Catalog, Expression Systems and Vectors, pp. 39-61.
Li et al.,The Journal of Biological Chemistry, 273(52):34970-34975 (Dec. 25, 1998).
Loetscher et al.,The Journal of Biological Chemistry, 266(17):11213-11220 (1991).
Moradpour et al., Characterization of Cell Lines Allowing Tightly Regulated Expression of Hepatitis C Virus Core Protein,Virology222:51-63 (1996).
Rechsteiner et al.,Cell Biology, 1:435-440 (1990).

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