Abstract
The characterization of the manner in which specific proteins interact is of immense interest not only for basic research but also for therapeutic research purposes. The identification of bioactive peptides can lead to new drug and therapeutic leads in biological systems in which proteins interact (e.g. signal transduction, protein targeting, cell cycle control). The identification of interacting peptides within multi-protein assemblies can also aid in the design of further experiments (e.g. mutagenesis, functional competition with peptides/domains) or the generation of computer models of the manner in which the proteins interact.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Brix J, Ziegler GA, Dietmeier K, Schneider-Mergener J, Schulz GE, Pfanner N (2000) The mitochondrial import receptor tom70: identification of a 25 kDa core domain with a specific binding site for preproteins. J Mol Biol 303: 479–88
DeLille J, Peterson EC, Johnson T, Moore M, Kight A, Henry R (2000) A novel precursor recognition element facilitates posttranslational binding to the signal recognition particle in chloroplasts. Proc Natl Acad Sci USA 97: 1926–31
Frank R (1992) SPOT synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron 48: 9217–9232
Franklin AE, Hoffman NE (1993) Characterisation of a chloroplast homologue of the 54-kDa subunit of the signal recognition particle. J Biol Chem 268: 22175–22180
Groves MR, Mant A, Kuhn A, Koch J, Dubel S, Robinson C, Sinning I (2001) Functional characterization of recombinant chloroplast signal recognition particle. J Biol Chem 276: 27778–86
High S, Henry R, Mould RM, Valent Q, Meacock S, dine K, Gray JC, Luirink J (1997) Chloroplast SRP54 interacts with a specific subset of thylakoid precursor proteins. J Biol Chem 272: 11622–11628
Hilpert K, Behlke J, Scholz C, Misselwitz R, Schneider-Mergener J, Höhne W (1999) Interaction of the capsid protein p24 (HIV-1) with sequenced-derived peptides: influence on p24 dimerization. Virology 254: 6–10
Hoffman NE, Franklin AE (1994) Evidence for a stromal GTP requirement for the integration of a chlorophyll a/b-binding polypeptide into thylakoid membranes. Plant Physiol 105: 295–304
Klimyuk VI, Persello-Cartieaux F, Havaux M, Contard-David P, Schuenemann D, Meiherhoff K, Gouet P, Jones JD, Hoffman NE, Nussaume L (1999) A chromodomain protein encoded by the Arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting. Plant Cell 11: 87–99
Knoblauch NT, Rudiger S, Schonfeld HJ, Driessen AJ, Schneider-Mergener J, Bukau B (1999) Substrate specificity of the SecB chaperone. J Biol Chem 274: 34219–25
Korth C, Stierli B, Streit P, Moser M, Schaller O, Fischer R, Schulz-Schaeffer W, Kretzschmar H, Raeber A, Braun Ehrensperger F, Hornemann S, Glockshuber R, Riek R, Billeter M, Wuthrich K, Oesch B (1997) Prion ( PrPSc)specific epitope defined by a monoclonal antibody. Nature 390: 74–77
Kramer A, Keitel T, Höhne W, Schneider-Mergener J (1997) Molecular basis of binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody. Cell 91: 799–809
Krieg UC, Walter P, Johnson AE (1986) Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc Natl Acad Sci USA 83: 8604–8
Li X, Henry R,Yuan J, Cline K, Hoffman NE (1995) A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes. Proc Natl Acad Sci USA 92: 3789–93
Lütcke H (1995) Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur J Biochem 228: 531–50
McCarty J, Rüdiger S, Schönfeld HJ, Schneider-Mergener J, Nakahigashi K, Yura T, Buckau B (1996) Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria. J Mol Biol 256: 829–837
Piossek C, Schneider-Mergener J, Schirner M, Vakalopolou E, Germeroth L, Thierauch KH (1999) Vascular endothelial growth factor ( VEGF) receptor II-derived peptides inhibit VEGF. J Biol Chem 274: 5612–5619
Schuenemann D, Gupta S, Persello-Cartieaux F, Klimyuk VI, Jones JDG, Nussaume L, Hoffman NE (1998) A novel signal recognition particle targets light-harvesting proteins to the thylakoid membranes. Proc Natl Acad Sci USA 95: 10312–10316
Schultz J, Hoffmüller U, Ashurst J, Krause G, Schmieder PJ, Macias M, Schneider-Mergener J, Oschkinat H (1998) Specific interactions between the synthrophin PDZ domain and voltage-gated sodium channels. Nature Struct Biol 5: 19–24
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Groves, M.R., Sinning, I. (2002). Protein-Protein Interactions. In: Koch, J., Mahler, M. (eds) Peptide Arrays on Membrane Supports. Springer Lab Manuals. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-09229-3_6
Download citation
DOI: https://doi.org/10.1007/978-3-662-09229-3_6
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-07639-8
Online ISBN: 978-3-662-09229-3
eBook Packages: Springer Book Archive