scholarly journals Evidence that a Chloroplast Surface Protein Is Associated with a Specific Binding Site for the Precursor to the Small Subunit of Ribulose-1,5-Bisphosphate Carboxylase

1987 ◽  
Vol 85 (3) ◽  
pp. 780-785 ◽  
Author(s):  
Karen L. Cornwell ◽  
Kenneth Keegstra
Keyword(s):  
Binding Site ◽  
Specific Binding ◽  
Surface Protein ◽  
Small Subunit ◽  
Bisphosphate Carboxylase

scholarly journals Novel proliferative effect of phospholipase A2 in Swiss 3T3 cells via specific binding site.

1991 ◽  
Vol 266 (29) ◽  
pp. 19139-19141
Author(s):  
H. Arita ◽  
K. Hanasaki ◽  
T. Nakano ◽  
S. Oka ◽  
H. Teraoka ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Binding Site ◽  
Specific Binding ◽  
3T3 Cells ◽  
Proliferative Effect ◽  
Swiss 3T3

Identification of the SV2 protein receptor-binding site of botulinum neurotoxin type E

2013 ◽  
Vol 453 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Stefan Mahrhold ◽  
Jasmin Strotmeier ◽  
Consuelo Garcia-Rodriguez ◽  
Jianlong Lou ◽  
James D. Marks ◽  
...  
Keyword(s):  
Binding Site ◽  
Synaptic Vesicle ◽  
Specific Binding ◽  
Cell Surface Receptor ◽  
Vesicle Membrane ◽  
Receptor Binding Site ◽  
Binding Interface ◽  
Protein Receptor ◽  
Surface Receptor ◽  
Extended Surface

The highly specific binding and uptake of BoNTs (botulinum neurotoxins; A–G) into peripheral cholinergic motoneurons turns them into the most poisonous substances known. Interaction with gangliosides accumulates the neurotoxins on the plasma membrane and binding to a synaptic vesicle membrane protein leads to neurotoxin endocytosis. SV2 (synaptic vesicle glycoprotein 2) mediates the uptake of BoNT/A and /E, whereas Syt (synaptotagmin) is responsible for the endocytosis of BoNT/B and /G. The Syt-binding site of the former was identified by co-crystallization and mutational analyses. In the present study we report the identification of the SV2-binding interface of BoNT/E. Mutations interfering with SV2 binding were located at a site that corresponds to the Syt-binding site of BoNT/B and at an extended surface area located on the back of the conserved ganglioside-binding site, comprising the N- and C-terminal half of the BoNT/E-binding domain. Mutations impairing the affinity also reduced the neurotoxicity of full-length BoNT/E at mouse phrenic nerve hemidiaphragm preparations demonstrating the crucial role of the identified binding interface. Furthermore, we show that a monoclonal antibody neutralizes BoNT/E activity because it directly interferes with the BoNT/E–SV2 interaction. The results of the present study suggest a novel mode of binding for BoNTs that exploit SV2 as a cell surface receptor.

scholarly journals Oxidative phosphorylation. The specific binding of trimethyltin and triethyltin to rat liver mitochondria

1970 ◽  
Vol 118 (1) ◽  
pp. 171-179 ◽  
Author(s):  
W. N. Aldridge ◽  
B. W. Street
Keyword(s):  
Adipose Tissue ◽  
Oxidative Phosphorylation ◽  
Brown Adipose Tissue ◽  
Binding Site ◽  
Rat Liver ◽  
Specific Binding ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Affinity Constants ◽  
Brown Adipose

1. The binding of trimethyltin and triethyltin to rat liver mitochondria was determined and the results were analysed by the method of Scatchard (1949). 2. One binding site (site 1) has the correct characteristics for the site to which trimethyltin and triethyltin are attached when they inhibit oxidative phosphorylation. For each compound the concentration of site 1 is 0.8nmol/mg of protein and the ratios of their affinity constants are the same as the ratio of the concentrations inhibiting oxidative phosphorylation. 3. Binding site 1 is present in a fraction derived from mitochondria containing only 15% of the original protein. In this preparation ultrasonication rapidly destroyed site 1. 4. Dimethyltin and diethyltin do not prevent binding of triethyltin to rat liver mitochondria, whereas triethyl-lead does. 5. Trimethyltin and triethyltin bind to mitochondria from brown adipose tissue and the results indicate a binding site 1 similar to that in rat liver mitochondria. 6. The advantages and limitations of this approach to the study of inhibitors are discussed.

A short conserved sequence is involved in the light-inducibility of a gene encoding ribulose 1,5-bisphosphate carboxylase small subunit of pea

Nature ◽  
1985 ◽  
Vol 315 (6016) ◽  
pp. 200-204 ◽  
Author(s):  
Giorgio Morelli ◽  
Ferenc Nagy ◽  
Robert T. Fraley ◽  
Stephen G. Rogers ◽  
Nam-Hai Chua
Keyword(s):  
Small Subunit ◽  
Gene Encoding ◽  
Bisphosphate Carboxylase ◽  
Conserved Sequence ◽  
Light Inducibility
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