TY - JOUR
T1 - Dansylation of bacteriorhodopsin near the retinal attachment site
AU - Harris, G.
AU - Renthal, R.
AU - Tuley, J.
AU - Robinson, N.
N1 - Funding Information:
ACKNOWLEDGEMENTS We are grateful to Dr. Austen Riggs for help with the amino acid analysis shown in Table I. We thank the Robert A. Welch Foundation (grant AX-736 to R.R.), NIH (grant GM 25483 to R.R. and GM 25795 to N.R.) and NSF (grant PCM 7822732 to R.R.) for supporting parts of this work. G.H. was a Robert A. Welch Predoctoral Fellow, 1978-79.
PY - 1979/12/14
Y1 - 1979/12/14
N2 - The purple membrane of Halobacterium halobium was reacted with 5-dimethylaminonaphthalene-l-sulfonyl chloride (dansyl chloride) at pH 8.0. Chromophoric and functional properties of the product appear unaltered. Approximately 2 moles of dansyl group were incorporated per mole of bacteriorhodopsin, part bound to bacteriorhodopsin and part bound to lipids. Purification and fragmentation of the protein showed most of the dansyl modification in a fragment containing residues 33 to 56. Amino acid analysis indicates that the major dansylated site is lysine 40. We conclude that, contrary to published models, 1) bacteriorhodopsin folds in a way that exposes lysine 40 at the membrane surface, and 2) this side chain is not involved in the proton pump mechanism.
AB - The purple membrane of Halobacterium halobium was reacted with 5-dimethylaminonaphthalene-l-sulfonyl chloride (dansyl chloride) at pH 8.0. Chromophoric and functional properties of the product appear unaltered. Approximately 2 moles of dansyl group were incorporated per mole of bacteriorhodopsin, part bound to bacteriorhodopsin and part bound to lipids. Purification and fragmentation of the protein showed most of the dansyl modification in a fragment containing residues 33 to 56. Amino acid analysis indicates that the major dansylated site is lysine 40. We conclude that, contrary to published models, 1) bacteriorhodopsin folds in a way that exposes lysine 40 at the membrane surface, and 2) this side chain is not involved in the proton pump mechanism.
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U2 - 10.1016/0006-291X(79)91968-5
DO - 10.1016/0006-291X(79)91968-5
M3 - Article
C2 - 526291
AN - SCOPUS:0018639961
VL - 91
SP - 926
EP - 931
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -