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PMID: 2644135 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A 10 kDa polypeptide associated with the oxygen-evolving complex of photosystem II has a putative C-terminal non-cleavable thylakoid transfer domain.

FEBS letters ·Vol. 242 ·No. 2 ·1989-01-02 ·Pages 435-8

Webber AN, Packman LC, Gray JC

Abstract

The N-terminal amino acid sequence of the 10 kDa polypeptide associated with the oxygen-evolving complex of wheat photosystem II has been determined and shown to be homologous to the amino acid sequence of the product of the ST-LS1 gene from potato. The N-terminal sequence of the mature protein indicates that the polypeptide is synthesized with a 39 amino acid N-terminal presequence which is similar to chloroplast import sequences but which lacks a hydrophobic domain for transfer of the protein across the thylakoid membrane. The mature polypeptide has a C-terminal hydrophobic region which shows homology to the hydrophobic thylakoid transfer domain of other lumenal proteins and this hydrophobic region of the 10 kDa polypeptide is suggested to facilitate transfer of the protein across the thylakoid membrane.

MeSH Terms
Amino Acid Sequence Chlorophyll/analysis Light-Harvesting Protein Complexes Molecular Sequence Data Molecular Weight Oxygen/metabolism Photosynthesis Photosynthetic Reaction Center Complex Proteins Photosystem II Protein Complex Plant Proteins/analysis Solubility Triticum
Chemicals
Light-Harvesting Protein Complexes Photosynthetic Reaction Center Complex Proteins Photosystem II Protein Complex Plant Proteins Chlorophyll Oxygen
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Webber A N
Department of Botany, University of Cambridge, England.
Packman L C
Gray J C
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1989-01-02
Pages
435-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
Wellcome Trust · United Kingdom
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