PMID: 2119798Jul 3, 1990Paper

Use of the membrane-impermeable guanidinating reagent 2-S-[14C]thiuroniumethanesulfonate to demonstrate the orientation of light-harvesting proteins in Rhodobacter sphaeroides

Biochemistry
B S Hundle, W R Richards

Abstract

The radiolabeled guanidinating reagent 2-S-[14C]thiuroniumethanesulfonate reacts with the epsilon-amino groups of accessible lysyl residues of membrane proteins under relatively mild labeling conditions, yielding labeled homoarginyl residues. Model studies have shown that the resulting homoarginyl residues do act as new cleavage sites for trypsin, but only at a very slow rate of hydrolysis. The reagent has been shown to be impermeable to the intracytoplasmic membranes of Rhodobacter sphaeroides: when cytoplasmic-side-out chromatophores were treated with the reagent, it reacted with all four of the light-harvesting proteins, all of which have one or more lysyl residues on the N-terminal sides of their hydrophobic regions. However, when periplasmic-side-out vesicles, prepared by cytochrome c affinity chromatography, were treated with the guanidinating reagent, three of the light-harvesting proteins (B850 alpha, B850 beta, and B870 beta) were not labeled. The only light-harvesting protein to be labeled (B870 alpha) was the only one of the four to have a lysyl residue on the C-terminal side of its hydrophobic region. Guanidinated B870 alpha polypeptides from both the cytoplasmic-side-out chromatophores and the periplasmic-side-out ...Continue Reading

References

Aug 1, 1987·Journal of Bioenergetics and Biomembranes·M ForteC A Mannella
Feb 1, 1972·Photochemistry and Photobiology·J Aagaard, W R Sistrom
Jul 1, 1984·Hoppe-Seyler's Zeitschrift für physiologische Chemie·R TheilerH Zuber
Jan 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·R M BroglieR K Clayton
Oct 1, 1957·Archives of Biochemistry and Biophysics·L WEIL, M TELKA
Feb 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·G W BrudvigK Sauer

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