HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Matoba, S. Articles by Ogrydziak, D. M. Search for Related Content PubMed PubMed Citation Articles by Matoba, S. Articles by Ogrydziak, D. M. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 30, 18841-18847, July 24, 1998

Another Factor Besides Hydrophobicity Can Affect Signal Peptide Interaction with Signal Recognition Particle

From the Institute of Marine Resources, University of California, Davis, California 95616

Translocation of alkaline extracellular protease (AEP) into the endoplasmic reticulum of Yarrowia lipolytica is cotranslational and signal recognition particle (SRP)-dependent, whereas translocation of P17M AEP (proline to methionine at position 17, second amino acid in the pro-region) is posttranslational and SRP-independent. P17M signal peptide mutations that resulted in more rapid SRP-dependent translocation of AEP precursor were isolated. Most of these mutations significantly increased hydrophobicity, but the A12P/P17M mutation did not. The switch from SRP-dependent to SRP-independent translocation without a decrease in hydrophobicity (wild type to P17M) and restoration of SRP-dependent translocation without an increase in hydrophobicity (P17M to A12P/P17M) indicate that some factor(s) in addition to hydrophobicity determines selection of targeting pathway. Models of extended forms of wild type and A12P/P17M signal peptides are kinked, whereas the P17M signal peptide is relatively straight. Possibly the conformation/orientation of signal peptides at the ribosomal surface affects SRP binding and consequently the targeting route to the endoplasmic reticulum. Kinked signal peptides might approach SRP more closely more often. Most likely, these effects were only detectable because of the short length and low average hydrophobicity of the AEP signal peptide.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				D. Huber, D. Boyd, Y. Xia, M. H. Olma, M. Gerstein, and J. Beckwith Use of Thioredoxin as a Reporter To Identify a Subset of Escherichia coli Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation J. Bacteriol., May 1, 2005; 187(9): 2983 - 2991. [Abstract] [Full Text] [PDF]

				S. Anjos, A. Nguyen, H. Ounissi-Benkalha, M.-C. Tessier, and C. Polychronakos A Common Autoimmunity Predisposing Signal Peptide Variant of the Cytotoxic T-lymphocyte Antigen 4 Results in Inefficient Glycosylation of the Susceptibility Allele J. Biol. Chem., November 22, 2002; 277(48): 46478 - 46486. [Abstract] [Full Text] [PDF]

				D. C. O'Sullivan, T. A. M. Szestak, and J. M. Pell Regulation of IGF-I mRNA by GH: putative functions for class 1 and 2 message Am J Physiol Endocrinol Metab, August 1, 2002; 283(2): E251 - E258. [Abstract] [Full Text] [PDF]

				J. A. Newitt, N. D. Ulbrandt, and H. D. Bernstein The Structure of Multiple Polypeptide Domains Determines the Signal Recognition Particle Targeting Requirement of Escherichia coli Inner Membrane Proteins J. Bacteriol., August 1, 1999; 181(15): 4561 - 4567. [Abstract] [Full Text]

				J.-W. L. de Gier, P. A. Scotti, A. Saaf, Q. A. Valent, A. Kuhn, J. Luirink, and G. von Heijne Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli PNAS, December 8, 1998; 95(25): 14646 - 14651. [Abstract] [Full Text] [PDF]