NDLI: The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting in Escherichia coli

Content Provider	Journal of Biological Chemistry (JBC)
Author	Stanley, Nicola R. Palmer, Tracy Berks, Ben C.
Abstract	In Escherichia coli a subset of periplasmic proteins is exported through the Tat pathway to which substrates are directed by an NH2-terminal signal peptide containing a consensus SRRXFLK “twin arginine” motif. The importance of the individual amino acids of the consensus motif forin vivo Tat transport has been assessed by site-directed mutagenesis of the signal peptide of the Tat substrate pre-SufI. Although the invariant arginine residues are crucial for efficient export, we find that slow transport of SufI is still possible if a single arginine is conservatively substituted by a lysine residue. Thus, in at least one signal peptide context there is no absolute dependence of Tat transport on the arginine pair. The consensus phenylalanine residue was found to be a critical determinant for efficient export but could be functionally substituted by leucine, another amino acid with a highly hydrophobic side chain. Unexpectedly, the consensus lysine residue was found to retard Tat transport. These observations and others suggest that the sequence conservation of the Tat consensus motif is a reflection of the functional importance of the consensus residues. Tat signal peptides characteristically have positively charged carboxyl-terminal regions. However, changing the sign of this charge does not affect export of SufI.
Related Links	http://www.jbc.org/content/275/16/11591.abstract
Ending Page	11596
Starting Page	11591
Page Count	6
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	16
Volume Number	275
DOI	10.1074/jbc.275.16.11591
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2000-04-21
Access Restriction	Open
Subject Keyword	H-, and c-regions, NH2-, hydrophobic, and COOH-terminal regions, respectively (n-) Polyacrylamide gel electrophoresis (PAGE) MEMBRANE TRANSPORT STRUCTURE FUNCTION AND BIOGENESIS
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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