The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins

T. Higashijima, K. M. Ferguson, P. C. Sternweis, E. M. Ross, M. D. Smigel, A. G. Gilman

Research output: Contribution to journalArticle

130 Citations (Scopus)

Abstract

The intensity of the tryptophan fluorescence of the α subunits of guanine nucleotide-binding regulatory proteins increases when they bind guanosine 5'-O-(3-thio)triphosphate (GTYγS). The kinetics of the fluorescence enhancement and of the measured binding of [35S]GTPγS are well correlated. The addition of Mg2+ to the nucleotide-bound proteins causes a further, rapid increase in the fluorescence intensity. Similar effects result from exposure of the proteins to F- and Mg2+, and the required concentration of F- is reduced by the inclusion of Al3+. It is presumed that the more highly fluorescent state of the G protein α subunits represents their active conformation.

Original languageEnglish (US)
Pages (from-to)752-756
Number of pages5
JournalJournal of Biological Chemistry
Volume262
Issue number2
StatePublished - 1987

Fingerprint

Guanine Nucleotides
GTP-Binding Proteins
Carrier Proteins
Fluorescence
Ligands
Guanosine 5'-O-(3-Thiotriphosphate)
Proteins
Protein Subunits
Tryptophan
Conformations
Nucleotides
Kinetics

ASJC Scopus subject areas

  • Biochemistry

Cite this

The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins. / Higashijima, T.; Ferguson, K. M.; Sternweis, P. C.; Ross, E. M.; Smigel, M. D.; Gilman, A. G.

In: Journal of Biological Chemistry, Vol. 262, No. 2, 1987, p. 752-756.

Research output: Contribution to journalArticle

@article{12953931e7c347229dee6bcdf4f31f59,
title = "The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins",
abstract = "The intensity of the tryptophan fluorescence of the α subunits of guanine nucleotide-binding regulatory proteins increases when they bind guanosine 5'-O-(3-thio)triphosphate (GTYγS). The kinetics of the fluorescence enhancement and of the measured binding of [35S]GTPγS are well correlated. The addition of Mg2+ to the nucleotide-bound proteins causes a further, rapid increase in the fluorescence intensity. Similar effects result from exposure of the proteins to F- and Mg2+, and the required concentration of F- is reduced by the inclusion of Al3+. It is presumed that the more highly fluorescent state of the G protein α subunits represents their active conformation.",
author = "T. Higashijima and Ferguson, {K. M.} and Sternweis, {P. C.} and Ross, {E. M.} and Smigel, {M. D.} and Gilman, {A. G.}",
year = "1987",
language = "English (US)",
volume = "262",
pages = "752--756",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "2",

}

TY - JOUR

T1 - The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins

AU - Higashijima, T.

AU - Ferguson, K. M.

AU - Sternweis, P. C.

AU - Ross, E. M.

AU - Smigel, M. D.

AU - Gilman, A. G.

PY - 1987

Y1 - 1987

N2 - The intensity of the tryptophan fluorescence of the α subunits of guanine nucleotide-binding regulatory proteins increases when they bind guanosine 5'-O-(3-thio)triphosphate (GTYγS). The kinetics of the fluorescence enhancement and of the measured binding of [35S]GTPγS are well correlated. The addition of Mg2+ to the nucleotide-bound proteins causes a further, rapid increase in the fluorescence intensity. Similar effects result from exposure of the proteins to F- and Mg2+, and the required concentration of F- is reduced by the inclusion of Al3+. It is presumed that the more highly fluorescent state of the G protein α subunits represents their active conformation.

AB - The intensity of the tryptophan fluorescence of the α subunits of guanine nucleotide-binding regulatory proteins increases when they bind guanosine 5'-O-(3-thio)triphosphate (GTYγS). The kinetics of the fluorescence enhancement and of the measured binding of [35S]GTPγS are well correlated. The addition of Mg2+ to the nucleotide-bound proteins causes a further, rapid increase in the fluorescence intensity. Similar effects result from exposure of the proteins to F- and Mg2+, and the required concentration of F- is reduced by the inclusion of Al3+. It is presumed that the more highly fluorescent state of the G protein α subunits represents their active conformation.

UR - http://www.scopus.com/inward/record.url?scp=0023096422&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023096422&partnerID=8YFLogxK

M3 - Article

C2 - 3100518

AN - SCOPUS:0023096422

VL - 262

SP - 752

EP - 756

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 2

ER -