Characterisation of an Arabidopsis thaliana cDNA encoding a novel thylakoid lumen protein imported by the ΔpH-dependent pathway
Characterisation of an Arabidopsis thaliana cDNA encoding a novel thylakoid lumen protein imported by the ΔpH-dependent pathway
An Arabidopsis thaliana (L.) Heynh. cDNA encoding a novel 16-kDa protein (P16) of the chloroplast thylakoid lumen has been characterised. The function of the protein is unknown but it shares some sequence similarity with alpha allophycocyanins. P16 is synthesised with a bipartite, lumen-targeting presequence, and import experiments demonstrated that this protein follows the ΔpH-dependent pathway. Analysis of the thylakoid transfer peptide revealed two unusual features. Firstly, the key targeting determinant is predicted to be a twin-arginine followed by a highly hydrophobic residue two residues later, rather than at the third position as in most transfer peptides. Secondly, the C-terminal domain of the transfer peptide contains multiple charged residues which may help to prevent mistargeting by the Sec-type protein translocase.
Arabidopsis (protein transport), Chloro plast, Protein transport, Targeting signal, Thylakoid lumen
624-627
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Kieselbach, Thomas
6438ae2a-9a2b-410f-b2bc-463bcd5df636
Schröder, Wolfgang P.
e628f500-a065-4964-8c78-28b2c4ab8709
Robinson, Colin
678e0157-d628-44e8-83de-3591b07c673f
February 1999
Mant, Alexandra
63319e45-deeb-45ad-a30d-e05b42052a0d
Kieselbach, Thomas
6438ae2a-9a2b-410f-b2bc-463bcd5df636
Schröder, Wolfgang P.
e628f500-a065-4964-8c78-28b2c4ab8709
Robinson, Colin
678e0157-d628-44e8-83de-3591b07c673f
Mant, Alexandra, Kieselbach, Thomas, Schröder, Wolfgang P. and Robinson, Colin
(1999)
Characterisation of an Arabidopsis thaliana cDNA encoding a novel thylakoid lumen protein imported by the ΔpH-dependent pathway.
Planta, 207 (4), .
(doi:10.1007/s004250050527).
Abstract
An Arabidopsis thaliana (L.) Heynh. cDNA encoding a novel 16-kDa protein (P16) of the chloroplast thylakoid lumen has been characterised. The function of the protein is unknown but it shares some sequence similarity with alpha allophycocyanins. P16 is synthesised with a bipartite, lumen-targeting presequence, and import experiments demonstrated that this protein follows the ΔpH-dependent pathway. Analysis of the thylakoid transfer peptide revealed two unusual features. Firstly, the key targeting determinant is predicted to be a twin-arginine followed by a highly hydrophobic residue two residues later, rather than at the third position as in most transfer peptides. Secondly, the C-terminal domain of the transfer peptide contains multiple charged residues which may help to prevent mistargeting by the Sec-type protein translocase.
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Published date: February 1999
Keywords:
Arabidopsis (protein transport), Chloro plast, Protein transport, Targeting signal, Thylakoid lumen
Identifiers
Local EPrints ID: 413071
URI: http://eprints.soton.ac.uk/id/eprint/413071
ISSN: 0032-0935
PURE UUID: bdb6307c-3af9-4826-86a1-72dc59ca1b06
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Date deposited: 14 Aug 2017 16:31
Last modified: 16 Mar 2024 03:40
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Contributors
Author:
Alexandra Mant
Author:
Thomas Kieselbach
Author:
Wolfgang P. Schröder
Author:
Colin Robinson
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