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GTP-binding proteins in plants
Cellular and Molecular Life Sciences CMLS, 1999GTP-binding proteins are found in all organisms. They are important switches that cycle between an active and an inactive state, ensuring vectorial flow of information on the expense of guanosine triphosphate (GTP). In this review, we discuss current progress in the molecular characterization and functional analysis of plant genes encoding ...
F, Bischoff +3 more
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Physiological Reviews, 2001
Small GTP-binding proteins (G proteins) exist in eukaryotes from yeast to human and constitute a superfamily consisting of more than 100 members. This superfamily is structurally classified into at least five families: the Ras, Rho, Rab, Sar1/Arf, and Ran families.
Y, Takai, T, Sasaki, T, Matozaki
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Small GTP-binding proteins (G proteins) exist in eukaryotes from yeast to human and constitute a superfamily consisting of more than 100 members. This superfamily is structurally classified into at least five families: the Ras, Rho, Rab, Sar1/Arf, and Ran families.
Y, Takai, T, Sasaki, T, Matozaki
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GTP-binding proteins in plants
Plant Molecular Biology, 1993Abstract Full length cDNAs of small GTP-binding proteins were inserted into PGEM1 under the control of the T7 promotor as described previously (Chavrier et al. 1990; Huber et al. 1993). GTP-binding proteins were then transiently expressed in BHK 21 cells with the T7 RNA polymeraserecombinant vaccinia virus system (Fuerst et al.
Terryn, N. +2 more
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The Rheb family of GTP-binding proteins
Cellular Signalling, 2004Rheb proteins represent a novel and unique family of the Ras superfamily GTP-binding proteins that is conserved from yeast to human. Biochemical studies establish that they bind and hydrolyze GTP. Molecular modeling studies reveal a few structural differences between Rheb and Ras, which may suggest that residues involved in biochemical activities ...
Paul-Joseph, Aspuria, Fuyuhiko, Tamanoi
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GTP-binding proteins in adrenocortical mitochondria
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995We have identified two GTP-binding proteins in mitochondria from bovine adrenal cortex (fasciculata). Sub-mitochondrial particles were fractionated into inner membrane, contact point and outer membrane vesicles on sucrose density gradients. These sub-mitochondrial fractions were identified by the presence of enzyme markers and electron microscopy ...
M, Thomson, M, Korn, P F, Hall
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Subunit interactions of GTP‐binding proteins
European Journal of Biochemistry, 1992Fluorescence energy transfer [cf. Förster, T. (1948) Ann. Phys. 6, 55–75] was tested for its suitability to study quantitative interactions of subunits of Go with each other and these subunits or trimeric Go with the β1‐adrenoceptor in detergent micelles or after reconstitution into lipid vesicles [according to Feder, D., Im, M.‐J., Klein, H.
Heithier, H. +9 more
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The International Journal of Biochemistry & Cell Biology, 1997
RhoA, RhoB and RhoC are three closely related proteins, and are members of the Ras super-family of small GTP-binding proteins. They bind and hydrolyse GTP, and are active in the GTP-bound form. Their activity in cells is regulated by exchange factors, GTPase activating proteins and guanine nucleotide dissociation inhibitors.
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RhoA, RhoB and RhoC are three closely related proteins, and are members of the Ras super-family of small GTP-binding proteins. They bind and hydrolyse GTP, and are active in the GTP-bound form. Their activity in cells is regulated by exchange factors, GTPase activating proteins and guanine nucleotide dissociation inhibitors.
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Current Opinion in Structural Biology, 1991
Abstract There has been much progress this year in characterizing the complex series of post-translational modifications important for GTP-binding protein function. In addition, the long-awaited molecular characterization of a G protein that regulates phospholipase C activity has been reported.
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Abstract There has been much progress this year in characterizing the complex series of post-translational modifications important for GTP-binding protein function. In addition, the long-awaited molecular characterization of a G protein that regulates phospholipase C activity has been reported.
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GTP-binding proteins in intracellular transport
Trends in Cell Biology, 1992One of the most exciting recent discoveries in the area of intracellular protein transport is the finding that many organelles involved in exocytic and endocytic membrane traffic have one or more Ras-like GTP-binding proteins on their cytoplasmic face that are specific for each membranous compartment.
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