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

Andrew Webber, Leonard C. Packman, John C. Gray

Research output: Contribution to journalArticle

23 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)435-438
Number of pages4
JournalFEBS Letters
Volume242
Issue number2
DOIs
StatePublished - Jan 2 1989
Externally publishedYes

Fingerprint

Thylakoids
Photosystem II Protein Complex
Thylakoid Membrane Proteins
Oxygen
Peptides
Amino Acids
Amino Acid Sequence Homology
Chloroplasts
Solanum tuberosum
Triticum
Amino Acid Sequence
Proteins
Genes

Keywords

  • (Wheat)
  • Chloroplast
  • Oxygen-evolving complex
  • Photosystem II
  • Presequence
  • Thylakoid transfer domain

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A 10 kDa polypeptide associated with the oxygen-evolving complex of photosystem II has a putative C-terminal non-cleavable thylakoid transfer domain. / Webber, Andrew; Packman, Leonard C.; Gray, John C.

In: FEBS Letters, Vol. 242, No. 2, 02.01.1989, p. 435-438.

Research output: Contribution to journalArticle

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N2 - 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.

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