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Sec-dependent thylakoid protein translocation: ΔpH requirement is dictated by passenger protein and ATP concentration

Sec-dependent thylakoid protein translocation: ΔpH requirement is dictated by passenger protein and ATP concentration
Sec-dependent thylakoid protein translocation: ΔpH requirement is dictated by passenger protein and ATP concentration

A Sec-type system is responsible for the translocation of a subset of proteins across the thylakoid membrane in higher plant chloroplasts. Previous studies have suggested that the thylakoidal ΔpH plays a minor role in this translocation mechanism, but we show here that it can be essential for the translocation process, depending on the identity of the passenger protein and the concentration of ATP. Studies using chimeric proteins show that, whereas the presequence dictates the translocation pathway, the ΔpH requirement is dictated exclusively by the passenger protein; some passenger proteins are virtually ΔpH-independent whereas others are absolutely dependent. ΔpH requirement is not related to charge characteristics of the passenger proteins, ruling out an electrophoretic effect. Analysis of the 33-kDa photosystem II protein reveals an inverse relationship between ΔpH requirement and ATP concentration; import into isolated thylakoids is inhibited 14-fold by nigericin at moderate ATP concentrations, and totally inhibited when the ATP concentration is reduced to 2 μM. The results indicate that the roles of the ΔpH and ATP overlap and suggest that the ΔpH may be obligatory when the passenger protein is abnormally difficult to translocate, possibly due to the folding of the polypeptide chain. We compare the energetics of this system with those of prokaryotic systems from which the chloroplast system is believed to have evolved.

0021-9258
23275-23281
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Schmidt, Ines
1d98fa0c-6428-4de1-829b-624342ffefbd
Herrmann, Reinhold G.
cb2f3159-3f73-4ca2-84be-23d44c17b81e
Klösgen, Ralf Bernd
1ddc41f6-e95a-4c64-be98-431fb814b58c
Robinson, Colin
678e0157-d628-44e8-83de-3591b07c673f
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Schmidt, Ines
1d98fa0c-6428-4de1-829b-624342ffefbd
Herrmann, Reinhold G.
cb2f3159-3f73-4ca2-84be-23d44c17b81e
Klösgen, Ralf Bernd
1ddc41f6-e95a-4c64-be98-431fb814b58c
Robinson, Colin
678e0157-d628-44e8-83de-3591b07c673f

Mant, Alexandra, Schmidt, Ines, Herrmann, Reinhold G., Klösgen, Ralf Bernd and Robinson, Colin (1995) Sec-dependent thylakoid protein translocation: ΔpH requirement is dictated by passenger protein and ATP concentration. The Journal of Biological Chemistry, 270 (40), 23275-23281. (doi:10.1074/jbc.270.40.23275).

Record type: Article

Abstract

A Sec-type system is responsible for the translocation of a subset of proteins across the thylakoid membrane in higher plant chloroplasts. Previous studies have suggested that the thylakoidal ΔpH plays a minor role in this translocation mechanism, but we show here that it can be essential for the translocation process, depending on the identity of the passenger protein and the concentration of ATP. Studies using chimeric proteins show that, whereas the presequence dictates the translocation pathway, the ΔpH requirement is dictated exclusively by the passenger protein; some passenger proteins are virtually ΔpH-independent whereas others are absolutely dependent. ΔpH requirement is not related to charge characteristics of the passenger proteins, ruling out an electrophoretic effect. Analysis of the 33-kDa photosystem II protein reveals an inverse relationship between ΔpH requirement and ATP concentration; import into isolated thylakoids is inhibited 14-fold by nigericin at moderate ATP concentrations, and totally inhibited when the ATP concentration is reduced to 2 μM. The results indicate that the roles of the ΔpH and ATP overlap and suggest that the ΔpH may be obligatory when the passenger protein is abnormally difficult to translocate, possibly due to the folding of the polypeptide chain. We compare the energetics of this system with those of prokaryotic systems from which the chloroplast system is believed to have evolved.

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Published date: 6 October 1995

Identifiers

Local EPrints ID: 413060
URI: https://eprints.soton.ac.uk/id/eprint/413060
ISSN: 0021-9258
PURE UUID: a2b9299a-7167-4996-8d41-497cb2fa4fb2
ORCID for Alexandra Mant: ORCID iD orcid.org/0000-0001-7169-209X

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Date deposited: 14 Aug 2017 16:31
Last modified: 13 Jun 2019 00:35

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Contributors

Author: Alexandra Mant ORCID iD
Author: Ines Schmidt
Author: Reinhold G. Herrmann
Author: Ralf Bernd Klösgen
Author: Colin Robinson

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