UNSPECIFIED (1998) Targeting of thylakoid proteins by the Delta pH-driven twin-arginine translocation pathway requires a specific signal in the hydrophobic domain in conjunction with the twin-arginine motif. FEBS LETTERS, 434 (3). pp. 425-430. ISSN 0014-5793

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Abstract

Superficially similar cleavable targeting signals specify whether lumenal proteins are transported across the thylakoid membrane by a Sec- or Delta pH-dependent pathway, A twin-arginine motif is essential but not sufficient to direct Delta pH-dependent targeting; here we show that a second determinant is located in the hydrophohic region. A highly hydrophobic amino acid is found either two or three residues C-terminal to the twin-arginine in all known transfer peptides for the Delta pH-dependent system, and substitution of this residue in the 23-kDa (23K) peptide markedly inhibits translocation, Further, whereas the insertion of twin-arginine in a Sec-dependent precursor does not permit efficient Delta pH-dependent targeting, the simultaneous presence of a leucine at the +3 position (relative to the RR) enables the peptide to function as efficiently as an authentic transfer peptide. RRNVL, RRAAL and RRALA within a Sec targeting signal all support efficient Delta pH-dependent targeting, RRNVA is less effective and RRNAA/RRNAG are totally ineffective, We conclude that the core signal for this pathway is a twin-arginine together with an adjacent hydrophobic determinant, (C) 1998 Federation of European Biochemical Societies.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	FEBS LETTERS
Publisher:	ELSEVIER SCIENCE BV
ISSN:	0014-5793
Date:	4 September 1998
Volume:	434
Number:	3
Number of Pages:	6
Page Range:	pp. 425-430
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/15361

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