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Signal Peptides 323 192. Beck, K. et al., Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor, EMBO J., 19, 134, 2000. 193. Delgado–Partin, V.M. and Dalbey, R.E., The protein motive force, acting on acidic residues, promotes translocation of amino-terminal domains of membrane proteins when the hydrophiobicity of the translocation signal is low, J. Biol. Chem., 273, 9927, 1998. 194. Rösch, K. et al., The topogenic contribution of uncharged amino acids on signal sequence orientation in the endoplasmic reticulum, J. Biol. Chem., 275, 14916, 2000. 195. Wahlberg, J.M. and Spiess, M., Multiple determinants direct the orientation of signalanchor proteins: the topogenic role of the hydrophobic signal domain, J. Cell Biol., 137, 555, 1997. 196. Cristóbal, S. et al., Competition between Sec- and TAT-dependent protein translocation in Eschericha coli, EMBO J., 18, 2982, 1999. 197. Chaddock, A.M. et al., A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the ∆pH-dependent thylakoidal protein translocase, EMBO J., 14, 2715, 1995. 198. Brink, S. et al., Targeting of thylakoid proteins by the ∆pH-driven twin-arginine translocation pathway requires a specific signal in the hydrophobic domain in conjunction with the two-arginine motif, FEBS Lett., 434, 425, 1998. 199. Stanley, N.R., Palmer, T., and Berks, B.C., The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli, J. Biol. Chem., 275, 11591, 2000. 200. Hinsley, A.P. et al., A naturally occurring bacterial Tat signal peptide lacking one of the “invariant” arginine residues of the consensus targeting motif, FEBS Lett., 497, 45, 2001. 201. Mori, H. and Cline, K., A signal peptide that directs non-Sec transport in bacteria also directs efficient and exclusive transport on the thylakoid ∆pH pathway, J. Biol. Chem., 273, 11405, 1998. 202. Blaudeck, N. et al., Specificity of signal peptide recognition in tat-dependent bacterial protein translocation, J. Bacteriol., 183, 604, 2001. 203. Bogsch, E., Brink, S., and Robinson, C., Pathway specificity for a ∆pH-dependent precursor thylakoid lumen protein is governed by a “Sec-avoidance” motif in the transfer peptide and a “Sec-incompatible” mature protein, EMBO J., 16, 3851, 1997. 204. Ng, T.W., Brown, J.D., and Walter, P., Signal sequences specify the targeting route to the endoplasmic reticulum membrane, J. Cell Biol., 134, 269, 1996. 205. Matoba, S. and Ogrydziak, D.M., Another factor besides hydrophobicity can affect signal peptide interaction with signal recognition particle, J. Biol. Chem., 273, 18841, 1998. 206. Zheng, T. and Nicchitta, C.V., Structural determinants for signal sequence function in the mammalian endoplasmic reticulum, J. Biol. Chem., 274, 36623, 1999. 207. Kyte, J. and Doolittle, R.F., A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157, 105, 1982. 208. Bannai, H. et al., Extensive feature detection of N-terminal protein sorting signals, Bioinformatics, 18, 298, 2002. 209. Claros, M.G., Brunak, S., and von Heijne, G., Prediction of N-terminal protein sorting signals, Curr. Opin. Struct. Biol., 7, 394, 1997. 210. Nielsen, H., Brunak, S., and von Heijne, G., Machine learning approaches for the prediction of signal peptides and other protein sorting signals, Protein Eng., 12, 3, 1999.
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CELL- PENETRATING PEPTIDES Processe
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Pharmacology and Toxicology: Basic
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Library of Congress Cataloging-in-P
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to the handbook are prominent resea
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REFERENCES 1. Green, M. and Loewens
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Contributors Mats Andersson Microbi
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Erin T. Pelkey Department of Chemis
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Contents Section I Classes of Cell-
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Chapter 16 Cell-Penetrating Peptide
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The Tat-Derived Cell-Penetrating Pe
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24 Cell-Penetrating Peptides: Proce
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3 Transportans Margus Pooga, Mattia
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Transportans 55 Indeed, galparan is
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Transportans 57 especially the endo
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Transportans 59 In the penetration
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Transportans 61 A 21-mer antisense
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Transportans 63 Commonly, the prote
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Transportans 65 antibiotin antibodi
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Transportans 67 For cross-linking o
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Transportans 69 and still retain ef
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Model Amphipathic Peptides 73 its D
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Model Amphipathic Peptides 75 pmol/
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TABLE 4.1 Internalization of Peptid
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TABLE 4.2 Internalization of Peptid
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Model Amphipathic Peptides 81 relat
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Model Amphipathic Peptides 87 A cat
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Model Amphipathic Peptides 89 At th
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Model Amphipathic Peptides 91 16. H
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Signal Sequence-Based Cell-Penetrat
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116 Cell-Penetrating Peptides: Proc
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Interactions of Cell-Penetrating Pe
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Structure Prediction of CPPs and It
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FIGURE 9.7 (Color Figure 9.7 follow
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FIGURE 9.8 The center of the figure
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Biophysical Studies of Cell-Penetra
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Toxicity and Side Effects of Cell-P
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Microbial Membrane-Permeating Pepti
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Index A Abaecin, 129 Abz radiolabel
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Index 399 Diffraction, 168 Disulphi
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Index 401 structure prediction, 187
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Index 403 pRB proteins, Tat-E1A bin
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Index 405 lipid perturbation (secon
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