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Unusual characteristics of amino-terminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides

Unusual characteristics of amino-terminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides
Unusual characteristics of amino-terminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides

Thylakoid transfer signals carry information specifying translocation by either a Sec- or ΔpH-dependent protein translocator in the chloroplast thylakoid membrane, yet all resemble classical signal peptides in overall structural terms. Comparison of known transfer signals reveals two differences: (a) signals for the ΔpH-driven system invariably contain a critical twin-argrinine (Arg-Arg) motif prior to the hydrophobic (H) domain, whereas known Sec-dependent signals contain lysine, and (b) the H-domains of Sec-dependent signals are generally longer. Previous work has shown that a twin-Arg motif before the H-domain is critical for targeting by the ΔpH-dependent pathway; in this report we show that the charge characteristics of this region are not important for sorting by the Sec pathway. Twin-Lys, twin-Am or single Arg are all acceptable to the Sec system, although single Lys/Arg is preferred. The single Lys in pre-plastocyanin can even be replaced by an uncharged residue without apparent effect. We have also generated a pre-plastocyanin mutant containing an H-domain which, in terms of hydropathy profile, is identical to that of a ΔpH-dependent protein. This mutant is also transported efficiently by the Sec system, demonstrating that hydrophobicity per se is not a key sorting determinant. However, the characteristics of the H-domain may be important in avoiding a different form of mis-targeting: to the endoplasmic reticulum. Thylakoid signal peptides have undergone substantial structural changes during the evolution of the chloroplast from endosymbiotic cyanobacterium: plastid-encoded and cyanobacterial signals contain H-domains that are highly hydrophobic and enriched in Leu and aromatic residues, whereas nuclear-encoded counterparts are Ala-rich and far less hydrophobic. We speculate that this trend may reflect a need to avoid mistargeting through recognition by cytosolic signal recognition particle, which preferentially interacts with more hydrophobic signal peptides.

Chloroplast, Protein transport, Signal peptide, Thylakoid
0014-2956
340-348
Brink, Susanne
7a46ec0b-0965-49c5-936e-64f3cd000769
Bogsch, Erik G.
1474b710-9d07-4db4-8f01-b1d4c8757105
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Robinson, Colin
678e0157-d628-44e8-83de-3591b07c673f
Brink, Susanne
7a46ec0b-0965-49c5-936e-64f3cd000769
Bogsch, Erik G.
1474b710-9d07-4db4-8f01-b1d4c8757105
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Robinson, Colin
678e0157-d628-44e8-83de-3591b07c673f

Brink, Susanne, Bogsch, Erik G., Mant, Alexandra and Robinson, Colin (1997) Unusual characteristics of amino-terminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides. European Journal of Biochemistry, 245 (2), 340-348. (doi:10.1111/j.1432-1033.1997.00340.x).

Record type: Article

Abstract

Thylakoid transfer signals carry information specifying translocation by either a Sec- or ΔpH-dependent protein translocator in the chloroplast thylakoid membrane, yet all resemble classical signal peptides in overall structural terms. Comparison of known transfer signals reveals two differences: (a) signals for the ΔpH-driven system invariably contain a critical twin-argrinine (Arg-Arg) motif prior to the hydrophobic (H) domain, whereas known Sec-dependent signals contain lysine, and (b) the H-domains of Sec-dependent signals are generally longer. Previous work has shown that a twin-Arg motif before the H-domain is critical for targeting by the ΔpH-dependent pathway; in this report we show that the charge characteristics of this region are not important for sorting by the Sec pathway. Twin-Lys, twin-Am or single Arg are all acceptable to the Sec system, although single Lys/Arg is preferred. The single Lys in pre-plastocyanin can even be replaced by an uncharged residue without apparent effect. We have also generated a pre-plastocyanin mutant containing an H-domain which, in terms of hydropathy profile, is identical to that of a ΔpH-dependent protein. This mutant is also transported efficiently by the Sec system, demonstrating that hydrophobicity per se is not a key sorting determinant. However, the characteristics of the H-domain may be important in avoiding a different form of mis-targeting: to the endoplasmic reticulum. Thylakoid signal peptides have undergone substantial structural changes during the evolution of the chloroplast from endosymbiotic cyanobacterium: plastid-encoded and cyanobacterial signals contain H-domains that are highly hydrophobic and enriched in Leu and aromatic residues, whereas nuclear-encoded counterparts are Ala-rich and far less hydrophobic. We speculate that this trend may reflect a need to avoid mistargeting through recognition by cytosolic signal recognition particle, which preferentially interacts with more hydrophobic signal peptides.

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More information

Published date: April 1997
Keywords: Chloroplast, Protein transport, Signal peptide, Thylakoid

Identifiers

Local EPrints ID: 413064
URI: https://eprints.soton.ac.uk/id/eprint/413064
ISSN: 0014-2956
PURE UUID: 64673944-6e71-48cc-9b44-20dc19c764a1

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Date deposited: 14 Aug 2017 16:31
Last modified: 13 Mar 2019 20:14

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Contributors

Author: Susanne Brink
Author: Erik G. Bogsch
Author: Alexandra Mant
Author: Colin Robinson

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