Specific guanine nucleotide binding by membranes from cucurbita pepo seedlings

M. Jacobs; M. P. Thelen; R. W. Famdale; M. C. Astle; P. H. Rubery

doi:10.1016/S0006-291X(88)81308-1

Specific guanine nucleotide binding by membranes from cucurbita pepo seedlings

M. Jacobs, M. P. Thelen, R. W. Famdale, M. C. Astle, P. H. Rubery

Research output: Contribution to journal › Article › peer-review

49 Scopus citations

Abstract

A microsomal membrane preparation from hypocotyls of dark-grown Cucurbita pepo L. (zucchini) seedlings contains specific high-affinity binding sites for the non-hydrolyzable GTP analog guanosine 5′-[γ-thio]triphosphate (GTP-γ-S). Both the binding affinity and the pattern of binding specificity for GTP and guanine nucleoside triphosphate analogs are shared with the more thoroughly characterized animal G-proteins that are known to be involved in signal transduction. The sensitivity of GTP-γ-S binding to Mg⁺² ions and temperature was similar to that reported for rabbit liver G-protein, although the plant complex dissociated more readily. GTP-γ-S could be recovered unchanged from the binding complex. Proteins (M_r 33 and 50 kDa) present in zucchini membrane preparations were revealed by immunoblotting with antiserum specific for the a subunit of platelet G_s. These may be homologous to animal G-proteins.

Original language	English (US)
Pages (from-to)	1478-1484
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	155
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(88)81308-1
State	Published - Sep 30 1988
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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@article{278848d20cc84e6e80d3ee9e1f6f77b2,

title = "Specific guanine nucleotide binding by membranes from cucurbita pepo seedlings",

abstract = "A microsomal membrane preparation from hypocotyls of dark-grown Cucurbita pepo L. (zucchini) seedlings contains specific high-affinity binding sites for the non-hydrolyzable GTP analog guanosine 5′-[γ-thio]triphosphate (GTP-γ-S). Both the binding affinity and the pattern of binding specificity for GTP and guanine nucleoside triphosphate analogs are shared with the more thoroughly characterized animal G-proteins that are known to be involved in signal transduction. The sensitivity of GTP-γ-S binding to Mg+2 ions and temperature was similar to that reported for rabbit liver G-protein, although the plant complex dissociated more readily. GTP-γ-S could be recovered unchanged from the binding complex. Proteins (Mr 33 and 50 kDa) present in zucchini membrane preparations were revealed by immunoblotting with antiserum specific for the a subunit of platelet Gs. These may be homologous to animal G-proteins.",

author = "M. Jacobs and Thelen, {M. P.} and Famdale, {R. W.} and Astle, {M. C.} and Rubery, {P. H.}",

note = "Funding Information: ACKNOWLEDGEMENTS We are grateful to Dr. L.M. Allan who prepared and donated 1251 secondary antibody and to Dr. B.R. Martin for helpful discussions. Dr. A.A. Newton kindly gave samples of some nucleotides. The work was supported in part by National Science Foundation grant PCM 8314844 to MJ, who is also grateful to the John Simon Guggenheim Foundation for a Fellowship.",

year = "1988",

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doi = "10.1016/S0006-291X(88)81308-1",

language = "English (US)",

volume = "155",

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T1 - Specific guanine nucleotide binding by membranes from cucurbita pepo seedlings

AU - Jacobs, M.

AU - Thelen, M. P.

AU - Famdale, R. W.

AU - Astle, M. C.

AU - Rubery, P. H.

N1 - Funding Information: ACKNOWLEDGEMENTS We are grateful to Dr. L.M. Allan who prepared and donated 1251 secondary antibody and to Dr. B.R. Martin for helpful discussions. Dr. A.A. Newton kindly gave samples of some nucleotides. The work was supported in part by National Science Foundation grant PCM 8314844 to MJ, who is also grateful to the John Simon Guggenheim Foundation for a Fellowship.

PY - 1988/9/30

Y1 - 1988/9/30

N2 - A microsomal membrane preparation from hypocotyls of dark-grown Cucurbita pepo L. (zucchini) seedlings contains specific high-affinity binding sites for the non-hydrolyzable GTP analog guanosine 5′-[γ-thio]triphosphate (GTP-γ-S). Both the binding affinity and the pattern of binding specificity for GTP and guanine nucleoside triphosphate analogs are shared with the more thoroughly characterized animal G-proteins that are known to be involved in signal transduction. The sensitivity of GTP-γ-S binding to Mg+2 ions and temperature was similar to that reported for rabbit liver G-protein, although the plant complex dissociated more readily. GTP-γ-S could be recovered unchanged from the binding complex. Proteins (Mr 33 and 50 kDa) present in zucchini membrane preparations were revealed by immunoblotting with antiserum specific for the a subunit of platelet Gs. These may be homologous to animal G-proteins.

AB - A microsomal membrane preparation from hypocotyls of dark-grown Cucurbita pepo L. (zucchini) seedlings contains specific high-affinity binding sites for the non-hydrolyzable GTP analog guanosine 5′-[γ-thio]triphosphate (GTP-γ-S). Both the binding affinity and the pattern of binding specificity for GTP and guanine nucleoside triphosphate analogs are shared with the more thoroughly characterized animal G-proteins that are known to be involved in signal transduction. The sensitivity of GTP-γ-S binding to Mg+2 ions and temperature was similar to that reported for rabbit liver G-protein, although the plant complex dissociated more readily. GTP-γ-S could be recovered unchanged from the binding complex. Proteins (Mr 33 and 50 kDa) present in zucchini membrane preparations were revealed by immunoblotting with antiserum specific for the a subunit of platelet Gs. These may be homologous to animal G-proteins.

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JO - Biochemical and Biophysical Research Communications

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Specific guanine nucleotide binding by membranes from cucurbita pepo seedlings

Abstract

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