Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

An Arabidopsis thaliana protein homologous to cyanobacterial high-light-inducible proteins

Tools
- Tools
+ Tools

UNSPECIFIED (2000) An Arabidopsis thaliana protein homologous to cyanobacterial high-light-inducible proteins. PLANT MOLECULAR BIOLOGY, 42 (2). pp. 345-351. ISSN 0167-4412

Full text not available from this repository.

Abstract

An Arabidopsis thaliana cDNA clone encoding a novel 110 amino acid thylakoid protein has been sequenced. The in vitro synthesized protein is taken up by intact chloroplasts, inserted into the thylakoid membrane and the transit peptide is cleaved off during this process. The mature protein is predicted to contain 69 amino acids, to form one membrane-spanning alpha-helix and to have its N-terminus at the stromal side of the thylakoid membrane. The protein showed similarity to the LHC, ELIP and PsbS proteins of higher plants, but more pronounced to the high-light-inducible proteins (HLIPs) of cyanobacteria and red algae, to which no homologue previously has been detected in higher plants. As for HLIP and ELIP, high light increases the mRNA levels of the corresponding gene. Sequence comparisons indicate that the protein may bind chlorophyll and form dimers in the thylakoid membrane. The level of expression of the protein seems to be far lower than that of normal PSI and PSII subunits.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
S Agriculture > SB Plant culture
Journal or Publication Title: PLANT MOLECULAR BIOLOGY
Publisher: KLUWER ACADEMIC PUBL
ISSN: 0167-4412
Date: January 2000
Volume: 42
Number: 2
Number of Pages: 7
Page Range: pp. 345-351
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/13532

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

Email us: publications@warwick.ac.uk
Contact Details
About Us