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
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Proteolytic processing of imported chloroplast proteins

Tools
- Tools
+ Tools

Elderfield, Peter D. (1990) Proteolytic processing of imported chloroplast proteins. PhD thesis, University of Warwick.

[img]
Preview
PDF
WRAP_Theses_Elderfield_1990.pdf - Submitted Version - Requires a PDF viewer.

Download (3492Kb) | Preview
Official URL: http://webcat.warwick.ac.uk/record=b3224745~S15

Request Changes to record.

Abstract

Three proteins located in the thylakoid lumen, plastocyanin and the 23KDa and 33KDa oxygen evolving polypeptides of photosystem II, are synthesised in the cytoplasm as higher molecular weight precursors, with N-terminal transit peptides. Import of these proteins involves removal of the first part of the transit peptide by a stromal processing peptidase to yield an intermediate. Maturation, by removal of the remaining transit peptide is performed by a thylakoidal processing peptidase (TPP). TPP has been partially purified and characterised from pea thylakoids and found to be an integral thylakoid membrane protein with the active site on the lumenal (trans) side of the membrane. TPP has a molecular weight of less than 250 000 and is not associated with any supra-molecular complex. Partial purification has yielded ten bands on a Coomassie stained SDS-PAGE gel; however TPP has not been attributed to any of these bands.

TPP displays specificity for chloroplast protein precursors with transit peptides containing a thylakoid transfer domain; however, no species specificity is displayed. TPP exhibits similarities in reaction specificity to Escherichia coli leader peptidase (LEP) in that both peptidases cleave the same eukaryotic and bacterial precursor as well as cleaving higher plant lumenal precursors at the predicted cleavage site.

No standard protease inhibitor has been found to abolish TPP activity; however, a synthetic signal sequence polypeptide will inhibit TPP and LEP.

A thylakoidal endopeptidase (EPS) has been discovered which cleaves lumenal precursors to a size slightly larger than the mature size. EP5 displays different inhibitor sensitivities to TPP and is either a high molecular weight protein or associated with a supramolecular complex. EPS is assumed to be involved in the turnover of thylakoid proteins.

Item Type: Thesis (PhD)
Subjects: Q Science > QK Botany
Library of Congress Subject Headings (LCSH): Chloroplasts, Proteins, Escherichia coli, Signal peptidases
Official Date: 1990
Dates:
DateEvent
1990UNSPECIFIED
Institution: University of Warwick
Theses Department: Department of Biological Sciences
Thesis Type: PhD
Publication Status: Unpublished
Supervisor(s)/Advisor: Robinson, Colin, 1958-
Extent: xv, 158 leaves : illustrations
Language: eng

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

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