Orientation of the carboxyl terminus of the Na+/proline symport carrier in Escherichia coli

FEBS Letters
Y KomeijiY Anraku

Abstract

The orientation of the carboxyl terminal region of the Escherichia coli proline carrier in the cytoplasmic membrane was studied. The beta-galactosidase moiety of the PutP-LacZ fusion protein [(1987) J. Biol. Chem. 262, 14100-14104] was exposed outside the inside-out vesicles and inside the right-side-out vesicles. A site-directed antibody raised against a synthetic peptide corresponding to the putative carboxyl terminal region of the carrier reacted preferentially with the inside-out vesicles prepared from a wild-type proline carrier overproducing strain and less with the right-side-out vesicles. These results indicate that the carboxyl terminus of the proline carrier is exposed to the cytoplasmic side of the membrane.

References

Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Jun 1, 1987·Molecular & General Genetics : MGG·T NakaoY Anraku
Jan 1, 1985·The Journal of Membrane Biology·C C ChenT H Wilson
Mar 26, 1984·FEBS Letters·T TsuchiyaT Kawasaki
Jan 1, 1983·Methods in Enzymology·M B SigelW P VanderLaan

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Citations

Nov 1, 1993·FEMS Microbiology Reviews·G I VeldW N Konings
Oct 3, 1998·The Journal of Biological Chemistry·H JungR Schmid
Jan 26, 1996·The Journal of Biological Chemistry·E TurkE M Wright
Mar 15, 2001·Biochimica Et Biophysica Acta·H Jung
Mar 23, 1992·Biochimica Et Biophysica Acta·K HanadaY Anraku

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