Modification of the Phosphatidylcholine‐Transfer Protein from Bovine Liver with Butanedione and Phenyiglyoxal

Akeroyd, Robert; Lange, Louis G.; Westerman, Jan; Wirtz, K.W.A.

doi:10.1111/j.1432-1033.1981.tb06432.x

Cited by 19 publications

(3 citation statements)

References 40 publications

(35 reference statements)

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“…Some structural roles in the formation and stability of active conformation are suggested for this hydrophobic core of PBP, which contains no disulfide bonds. It has been shown that arginine residues have an important role in enzymes that act on phosphate-containing substrates (2,31,38). Among the four arginine residues of PBP, two consecutive arginine residues are localized at positions 109 and 110.…”

Section: Discussionmentioning

confidence: 99%

Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli

Magota¹,

Otsuji²,

Miki³

et al. 1984

J Bacteriol

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phoS is the structural gene for the phosphate-binding protein, which is localized in periplasm and involved in active transport of phosphate in Escherichia coli. It is also a negative regulatory gene for the pho regulon, and the gene expression is inducible by phosphate starvation. The complete nucleotide sequence of the phoS gene was determined by the method of Maxam and Gilbert (A. M. Maxam and W. Gilbert, Methods Enzymol. 65:499-560, 1980). The amino acid sequences at the amino termini of the pre-PhoS and PhoS proteins and at the carboxy terminus of the PhoS protein were determined by using the purified proteins. Furthermore, the amino acid sequence of enzymatically digested peptide fragments of the PhoS protein was determined. The combined data established the nucleotide sequence of the coding region and the amino acid sequence of the pre-PhoS and the PhoS proteins. The pre-PhoS protein contains an extension of peptide composed of 25 amino acid residues at the amino terminus of the PhoS protein, which has the general characteristics of a signal peptide. The mature PhoS protein is composed of 321 amino acid residues, with a calculated molecular weight of 34,422, and lacks the disulfide bond and methionine. The regulatory region of phoS contains a characteristic Shine-Dalgarno sequence at an appropriate position preceding the translational initiation site, as well as three possible Pribnow boxes and one-35 sequence. The nucleotide sequence of the regulatory region of phoS was compared with those of phoA and phoE, the genes constituting the pho regulon.

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Section: Discussionmentioning

confidence: 99%

Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli

Magota¹,

Otsuji²,

Miki³

et al. 1984

J Bacteriol

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“…To determine the number of j residues, many investigators have examined the effects of specific ligands on inactivation and modification of proteins [e.g. Akeroyd et al, 1981;Ramakrishna & Benjamin, 1981;Carrillo et al, 1981;Tso & Zalkin, 1981;Cromartie, 1981;Brooker & Slayman, 1983;Hennecke & Plapp, 1983; as well as the papers cited by Horiike & McCormick (1980) and Rakitzis (1984)]. In the absence and the presence of a ligand, the differences in both the nunmber of residues modified (m) and the fractional remaining activity (a), i.e.…”

Section: Bj-1 C Lettersmentioning

confidence: 99%

Effect of ligands on chemical modification of proteins

Horiike¹,

Tojo²,

Yamano³

et al. 1984

Biochemical Journal

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“…The cross-reactivity of bovine hFABP with corresponding proteins from rat and human liver has been considered already [4] and Northern blot analysis of bovine-hFABP mRNA was positive with synthetic oligonucleotides that were colinear with rat hFABP cDNA [32]. It is well known that essential Arg residues are found in proteins that act on phosphate-containing substrates [22, 33, 341, e. g. in phosphatidylcholine-transfer protein from bovine liver, one of the ten Arg residues interacts electrostatically with the polar head group of phosphatidylcholine [22]. We found no evidence that bovine hFABP binds this phospholipid [2, 111; however, the binding of lysophosphatidylcholine by rat hFABP was reported recently [35].…”

Section: Electrostatic Interactionsmentioning

confidence: 99%

Interactions of fatty acids with neutral fatty‐acid‐binding protein from bovine liver

Schulenberg‐Schell

Schäfer-Keller

Keuper

et al. 1988

European Journal of Biochemistry

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Hepatic‐type fatty‐acid‐binding protein (hFABP) from the cytosol of bovine liver is a 14.4‐kDa neutral protein with a blocked N‐terminus and a disulfide system located on the surface of the protein. It binds two molecules of fatty acid in one binding site, apparent dissociation constants of the oleic acid/hFABP complex are 0.24 μM and 2.15 μM. Computer analysis of circular dichroic spectra predicts that hFABP contains about 12%α‐helix, 45%β‐structure, 15%β‐turn and 27% unordered structure. Ellipticities indicative of secondary structure are not affected by fatty acid binding. Cationic amino acid residues of hFABP (1 His, 15 Lys, 2 Arg) were screened for ionic fatty acid/protein interactions. His was excluded, as 1H‐NMR analysis of His‐C2 and His‐C4 protons indicated that binding of oleic acid shifts the pK of His from 6.9 to 7.1 only in hFABP with the disulfide system in the oxidized state; acylation of His with diethylpyrocarbonate does not affect the binding of the fatty acid. Acetylation of Lys reduces binding marginally, whereas modification of Arg with phenylglyoxal lowers the binding activity by 65%. From 1H‐NMR investigations, conformational changes within the protein, due to a sort of disaggregation of hFABP upon fatty acid binding, were derived. Most of the proton resonances sharpen up with ligand binding, and some of the methyl resonances shift positions, possibly because they are directly involved in the fatty acid/protein interaction.

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Modification of the Phosphatidylcholine‐Transfer Protein from Bovine Liver with Butanedione and Phenyiglyoxal

Cited by 19 publications

References 40 publications

Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli

Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli

Effect of ligands on chemical modification of proteins

Interactions of fatty acids with neutral fatty‐acid‐binding protein from bovine liver

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