The gag homologue of retrotransposon Ty1 assembles into spherical particles in Escherichia coli.
Expression of TyA (reading frame A) of the yeast retrotransposon Ty1 in Escherichia coli is possible by using efficient transcriptional and translational initiation signals. When expressed in E. coli, the gag homologue of Ty1 assembles into spherical particles similar, but not identical to virus-like particles in the natural host of Ty1, Saccharomyces cerevisiae. Deletion analysis reveals a domain in the C-terminus of TyA that is essential for the assembly process. These findings indicate that an early step of the retroelement life cycle, assembly of the gag homologue into spherical particles, does not depend on specific host factors. The experiments also demonstrate that Ty1 Gag fusion proteins, potential tools for immunization, can be produced in E. coli, an organism that lacks endogenous retrotransposons.
Luschnig
C
C
Department of Cytology and Genetics, University of Vienna, Austria.
Hess
M
M
Pusch
O
O
Brookman
J
J
Bachmair
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D017931:DNA Primers; D004269:DNA, Bacterial; D004926:Escherichia coli / Q000235:genetics*; D015683:Gene Products, gag / Q000235:genetics* / Q000648:ultrastructure; D005822:Genetic Vectors; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016366:Open Reading Frames; D018626:Retroelements; D017384:Sequence Deletion
D017931:DNA Primers; D004269:DNA, Bacterial; D015683:Gene Products, gag; D018626:Retroelements