NDLI: Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries.

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Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries.

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Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Quinn, M. T. Yu, L. Jesaitis, A. J. Loetterle, L. R. Bond, C. W. Burritt, J. B. Deleo, F. R.
Description	Author Affiliation: DeLeo FR ( Department of Veterinary Molecular Biology, Montana State University, Bozeman 59717, USA.);
Abstract	During assembly of the phagocyte NADPH oxidase, cytosolic p47-phox translocates to the plasma membrane and binds to flavocytochrome b, and binding domains for p47-phox have been identified on the C-terminal tails of both flavocytochrome b subunits. In the present report, we further examine the interaction of these two oxidase components by using random-sequence peptide phage display library analysis. Screening p47-phox with the peptide libraries identified five potential sites of interaction with flavocytochrome b, including three previously reported regions of interaction and two additional regions of interaction of p47-phox with gp91-phox and p22-phox. The additional sites were mapped to a domain on the first predicted cytosolic loop of gp91-phox encompassing residues S86TRVRRQL93 and to a domain near the cytosolic C-terminal tail of gp91-phox encompassing residues F450EWFADLL457. The mapping also confirmed a previously reported binding domain on gp91-phox (E554SGPRGVHFIF564) and putative Src homology 3 domain binding sites on p22-phox (P156PRPP160 and G177GPPGGP183). To demonstrate that the additional regions identified were biologically significant, peptides mimicking the gp91-phox sequences F77LRGSSACCSTRVRRQL93 and E451WFADLLQLLESQ463 were synthesized and assayed for their ability to inhibit NADPH oxidase activity. These peptides had EC50 values of 1 microM and 230 microM, respectively, and inhibited activation when added prior to assembly but did not affect activity of the preassembled oxidase. Our data demonstrate the usefulness of phage display library analysis for the identification of biologically relevant sites of protein-protein interaction and show that the binding of p47-phox to flavocytochrome b involves multiple binding sites along the C-terminal tails of both gp91- and p22-phox and other regions of gp91-phox nearer to the N terminus.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochrome b Group Metabolism Membrane Transport Proteins NADH, NADPH Oxidoreductases Biosynthesis NADPH Dehydrogenase Neutrophils Enzymology Peptide Fragments Phosphoproteins Binding Sites Genetics Gene Library Membrane Glycoproteins Drug Effects NADPH Oxidase Pharmacology Protein Binding Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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