English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides

Francia, F., Wang, J., Zischka, H., Venturoli, G., & Oesterhelt, D. (2002). Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides. European Journal of Biochemistry, 269(7), 1877-1885.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Eur. J. Biochem.

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Francia, F.1, Author              
Wang, J.1, Author              
Zischka, H.1, Author              
Venturoli, G., Author
Oesterhelt, D.1, Author              
Affiliations:
1Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              

Content

show
hide
Free keywords: LH1-RC; photosynthesis; PufX; Rhodobacter sphaeroides
 Abstract: The core complex of Rhodobacter sphaeroides is formed by the association of the light-harvesting antenna 1 (LH1) and the reaction center (RC). The PufX protein is essential for photosynthetic growth; it is located within the core in a 1 : 1 stoichiometry with the RC. PufX is required for a fast ubiquinol exchange between the Q(B) site of the RC and the Qo site of the cytochrome bc(1) complex. In vivo the LH1-PufX-RC complex is assembled in a dimeric form, where PufX is involved as a structural organizer. We have modified the PufX protein at the N and the C-terminus with progressive deletions. The nine mutants obtained have been characterized for their ability for photosynthetic growth, the insertion of PufX in the core LH1-RC complex, the stability of the dimers and the kinetics of flash- induced reduction of cytochrome b(561) of the cytochrome bc(1) complex. Deletion of 18 residues at the N-terminus destabilizes the dimer in vitro without preventing photosynthetic growth. The dimer (or a stable dimer) does not seem to be a necessary requisite for the photosynthetic phenotype. Partial C-terminal deletions impede the insertion of PufX, while the complete absence of the C-terminus leads to the insertion of a PufX protein composed of only its first 53 residues and does not affect the photosynthetic growth of the bacterium. Overall, the results point to a complex role of the N and C domains in the structural organization of the core complex; the N-terminus is suggested to be responsible mainly for dimerization, while the C-terminus is thought to be involved mainly in PufX assembly.

Details

show
hide
Language(s): eng - English
 Dates: 2002-04
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 39206
ISI: 000174768600009
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: European Journal of Biochemistry
  Alternative Title : Eur. J. Biochem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 269 (7) Sequence Number: - Start / End Page: 1877 - 1885 Identifier: ISSN: 0014-2956