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Identification of an α Helical Motif Sufficient for Association with Papillomavirus E6

Chen, Jason J., Hong, Yihui, Rustamzadeh, Edward, Baleja, James D., Androphy, Elliot J.·1998·Journal of Biological Chemistry
DOI 10.1074/jbc.273.22.13537
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CC-BY · From the PDF
FIG. 2 Demonstration of calcium binding by E6 binding peptide by 1 H NMR spectroscopy. A , the metal-free peptide was at 1.0 mMconcentration in a solution containing 20 mM NaCl. B , addition of 80 mM calcium chloride (CaCl2 ) to the peptide induces chemical shift dispersion. The downfield-shifted resonance of glycine 17 is indicated with an arrow and is typical of a calcium-bound EF-hand. The addition of a small amount of TFE (5-10%) narrows some resonance line widths. Sample conditions were 1.0 mM peptide in a buffer containing 8% TFE, 20 mM NaCl, pH 6.0.
FIG. 2 Demonstration of calcium binding by E6 binding peptide by 1 H NMR spectroscopy. A , the metal-free peptide was at 1.0 mMconcentration in a solution containing 20 mM NaCl. B , addition of 80 mM calcium chloride (CaCl2 ) to the peptide induces chemical shift dispersion. The downfield-shifted resonance of glycine 17 is indicated with an arrow and is typical of a calcium-bound EF-hand. The addition of a small amount of TFE (5-10%) narrows some resonance line widths. Sample conditions were 1.0 mM peptide in a buffer containing 8% TFE, 20 mM NaCl, pH 6.0.CC-BY · From the PDF
FIG. 3 The NH-NH region of the two-dimensional NOESY spectrum. Resonance assignments were accomplished by tracing connections between the NH, a , and b protons of a residue ( i ), and the NH of the next residue ( i 1 1). The helical nature of this peptide is illustrated by medium and strong NH to NH NOE cross-peaks between residues adjacent in sequence. Sample conditions are given in Fig. 3, and the NOE mixing time was 125 ms.
FIG. 3 The NH-NH region of the two-dimensional NOESY spectrum. Resonance assignments were accomplished by tracing connections between the NH, a , and b protons of a residue ( i ), and the NH of the next residue ( i 1 1). The helical nature of this peptide is illustrated by medium and strong NH to NH NOE cross-peaks between residues adjacent in sequence. Sample conditions are given in Fig. 3, and the NOE mixing time was 125 ms.CC-BY · From the PDF
FIG. 4 Summaryof the conformational data. The sequence of the peptide, corresponding to residues 289-318 of E6BP, is renumbered as residues 1-31. The residues that ligate calcium are boxed . These residues form single ligands to calcium using their side chains, except for F18, which uses its backbone carbonyl, and E23, which contributes a double ligand. NOE cross-peaks describing NH-to-NH contacts, H a -NH contacts, H b -NH contacts, and H a to H b ( i 1 3) contacts are illustrated with the thickness of the filled-in bar corresponding to NOE intensity. The absence of a bar indicates that the NOE was not observed, whereas the presence of the dotted line indicates that the NOE was likely but was obscured by resonance overlap. A hollow bar indicates that the NOEinvolves a glycine residue and is not applicable. The chemical shift index ( CSI ) is positive if the difference in chemical shift between observed and a random coil peptide was greater than 0.1 ppm or negative if it was less than 0.1 ppm (61). A positive index indicates b sheet, whereas a negative index indicates a helix. A summary for the secondary structure of the peptide is shown under the conformational data.
FIG. 4 Summaryof the conformational data. The sequence of the peptide, corresponding to residues 289-318 of E6BP, is renumbered as residues 1-31. The residues that ligate calcium are boxed . These residues form single ligands to calcium using their side chains, except for F18, which uses its backbone carbonyl, and E23, which contributes a double ligand. NOE cross-peaks describing NH-to-NH contacts, H a -NH contacts, H b -NH contacts, and H a to H b ( i 1 3) contacts are illustrated with the thickness of the filled-in bar corresponding to NOE intensity. The absence of a bar indicates that the NOE was not observed, whereas the presence of the dotted line indicates that the NOE was likely but was obscured by resonance overlap. A hollow bar indicates that the NOEinvolves a glycine residue and is not applicable. The chemical shift index ( CSI ) is positive if the difference in chemical shift between observed and a random coil peptide was greater than 0.1 ppm or negative if it was less than 0.1 ppm (61). A positive index indicates b sheet, whereas a negative index indicates a helix. A summary for the secondary structure of the peptide is shown under the conformational data.CC-BY · From the PDF
FIG. 5 Model for the E6bp peptide. The peptide was modeled using the x-ray structure of the calcium-bound motif from troponin C. The helical elements are shown as cylinders . The side chains and backbone carbonyl groups that ligate the calcium ions are shown.
FIG. 5 Model for the E6bp peptide. The peptide was modeled using the x-ray structure of the calcium-bound motif from troponin C. The helical elements are shown as cylinders . The side chains and backbone carbonyl groups that ligate the calcium ions are shown.CC-BY · From the PDF
FIG. 6 An a helical motif is sufficient for association with E6. Glutathione-Sepharose beads containing GST-E6BP fusion proteins were combined with 35 S-labeled in vitro translated BPV-1 E6 proteins in LSAB. After incubation and washes, the bound products were separated by SDS-polyacrylamide gel electrophoresis. E6 binding was analyzed by Molecular Imager. A , construction of deletion and point mutations of E6bd GST fusion proteins. Numbers for binding are the percentage of association from each mutant normalized to the level seen with E6bd-M. The average of three independent experiments, including standard deviations, is given. B , an a helical motif is important for association with E6. The image of one representative experiment is shown. Sequences of the E6 binding domain (E6bd) 7 through 31 are given. Input was loaded directly into the well and represents 10% of the 35 S-labeled E6 used in each binding reaction.
FIG. 6 An a helical motif is sufficient for association with E6. Glutathione-Sepharose beads containing GST-E6BP fusion proteins were combined with 35 S-labeled in vitro translated BPV-1 E6 proteins in LSAB. After incubation and washes, the bound products were separated by SDS-polyacrylamide gel electrophoresis. E6 binding was analyzed by Molecular Imager. A , construction of deletion and point mutations of E6bd GST fusion proteins. Numbers for binding are the percentage of association from each mutant normalized to the level seen with E6bd-M. The average of three independent experiments, including standard deviations, is given. B , an a helical motif is important for association with E6. The image of one representative experiment is shown. Sequences of the E6 binding domain (E6bd) 7 through 31 are given. Input was loaded directly into the well and represents 10% of the 35 S-labeled E6 used in each binding reaction.CC-BY · From the PDF
FIG. 7 An a helix is conserved among E6-binding proteins. A , comparison of E6 binding domains reveals a conserved motif. The E6 binding peptides of E6bd (residues 18-29), the 18 amino acids (amino acids 391-408) of E6AP (2), and the sequence of LD1 from paxillin (amino acids 3-15) (3) are aligned. h , amino acid that can form a double hydrogen bond, i.e. Asp, Glu, Gln. X , any amino acid. f , hydrophobic amino acid. s , small amino acid such as Gly or Ala. 2 , acidic residue. B , amino acids in the second helix of the helix-loop-helix that comprise the EF-hand in a helical wheel representation. In E6BP, replacement of either Leu-21, Phe-24, Leu-25, or Asp 27 by Ala reduced binding to E6 by at least 10-fold. Alanine replacements of the Gly-26 results in about a 5-fold loss in binding, whereas replacement of the other residues did not appreciably affect binding. Left , the motif for E6BP (EF-hand 4). Center , the motif for E6AP. Right , an example of a nonbinding E6 motif (the homologous residues from EF-hand 5 of E6BP).
FIG. 7 An a helix is conserved among E6-binding proteins. A , comparison of E6 binding domains reveals a conserved motif. The E6 binding peptides of E6bd (residues 18-29), the 18 amino acids (amino acids 391-408) of E6AP (2), and the sequence of LD1 from paxillin (amino acids 3-15) (3) are aligned. h , amino acid that can form a double hydrogen bond, i.e. Asp, Glu, Gln. X , any amino acid. f , hydrophobic amino acid. s , small amino acid such as Gly or Ala. 2 , acidic residue. B , amino acids in the second helix of the helix-loop-helix that comprise the EF-hand in a helical wheel representation. In E6BP, replacement of either Leu-21, Phe-24, Leu-25, or Asp 27 by Ala reduced binding to E6 by at least 10-fold. Alanine replacements of the Gly-26 results in about a 5-fold loss in binding, whereas replacement of the other residues did not appreciably affect binding. Left , the motif for E6BP (EF-hand 4). Center , the motif for E6AP. Right , an example of a nonbinding E6 motif (the homologous residues from EF-hand 5 of E6BP).CC-BY · From the PDF

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Metadata

Authors
Chen, J. J., Hong, Y., Rustamzadeh, E., Baleja, J. D., & Androphy, E. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-05
Volume
273
Issue
22
Pages
13537-13544
ISSN
0021-9258
DOI
10.1074/jbc.273.22.13537
Cited by
93
References
1
Language
en
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