Identification of the high-affinity lipid binding site in Escherichia coli pyruvate oxidase

Biochemistry ◽  
1986 ◽  
Vol 25 (25) ◽  
pp. 8178-8183 ◽  
Author(s):  
Susan E. Hamilton ◽  
Michael Recny ◽  
Lowell P. Hager
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Lipid Binding ◽  
Pyruvate Oxidase ◽  
High Affinity ◽  
Lipid Binding Site

scholarly journals Hydrodynamic properties of colicin A. Existence of a high-affinity lipid-binding site and oligomerization at acid pH

1988 ◽  
Vol 172 (2) ◽  
pp. 507-512 ◽  
Author(s):  
Daniele CAVARD ◽  
Paul SAUVE ◽  
Frederic HEITZ ◽  
Franc PATTUS ◽  
Carmen MARTINEZ ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Hydrodynamic Properties ◽  
High Affinity ◽  
Acid Ph ◽  
Lipid Binding Site

The N-Terminus is the Lipid-Binding Site of SAA: Supporting Evidence by MoAbs

1991 ◽  
pp. 83-86
Author(s):  
Yifat Ziq-Bachar ◽  
David Levartowsky ◽  
Mordechaipras ◽  
Alistair F. Strachan ◽  
Mati Fridkin ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Supporting Evidence ◽  
N Terminus ◽  
Lipid Binding Site

Phosphorylation and DNA binding of the regulator DcuR of the fumarate-responsive two-component system DcuSR of Escherichia coli

Microbiology ◽  
2004 ◽  
Vol 150 (4) ◽  
pp. 877-883 ◽  
Author(s):  
Ingo G. Janausch ◽  
Inma Garcia-Moreno ◽  
Daniela Lehnen ◽  
Yvonne Zeuner ◽  
Gottfried Unden
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Response Regulator ◽  
Sensory System ◽  
Phosphoryl Transfer ◽  
Affinity Binding ◽  
High Affinity ◽  
Two Component ◽  
Target Promoters

The function of the response regulator DcuR of the DcuSR fumarate two-component sensory system of Escherichia coli was analysed in vitro. Isolated DcuR protein was phosphorylated by the sensory histidine kinase, DcuS, and ATP, or by acetyl phosphate. In gel retardation assays with target promoters (frdA, dcuB, dctA), phosphoryl DcuR (DcuR-P) formed a high-affinity complex, with an apparent K D (app. K D) of 0·2–0·3 μM DcuR-P, and a low-affinity (app. K D 0·8–2 μM) complex. The high-affinity complex was formed only with promoters transcriptionally-regulated by DcuSR, whereas low-affinity binding was seen also with some DcuSR-independent promoters. The binding site of DcuR-P at the dcuB promoter was determined by DNase I footprinting. One binding site of 42–52 nt (position −359 to −400/−410 nt upstream of the transcriptional start) was identified in the presence of low and high concentrations of DcuR-P. Non-phosphorylated DcuR, or DcuR-D56N mutated in the phosphoryl-accepting Asp56 residue, showed low-affinity binding to target promoters. DcuR-D56N was still able to interact with DcuS. DcuR-D56N increased the phosphorylation of DcuS and competitively inhibited phosphoryl transfer to wild-type DcuR.

Identification of the Lipid-Binding Site of Phosphatidylcholine-Transfer Protein with Phosphatidylcholine Analogs Containing Photactivable Carbene Precursors

1983 ◽  
Vol 132 (2) ◽  
pp. 441-449 ◽  
Author(s):  
Jan WESTERMAN ◽  
Karel W. A. WIRTZ ◽  
Theo BERKHOUT ◽  
Laurens L. M. DEENEN ◽  
Ramachandran RADHAKRISHNAN ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Transfer Protein ◽  
Phosphatidylcholine Transfer Protein ◽  
Lipid Binding Site
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