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

Localisation and interactions of the Vipp1 protein in cyanobacteria

Tools
- Tools
+ Tools

Bryan, Samantha J., Burroughs, Nigel John, Shevela, Dmitriy, Yu, Jianfeng, Rupprecht, Eva, Liu, Lu-Ning, Mastroianni, Giulia, Xue, Quan, Llorente-Garcia, Isabel, Leake, Mark C., Eichacker, Lutz A., Schneider, Dirk, Nixon, Peter J. and Mullineaux, Conrad W. (2014) Localisation and interactions of the Vipp1 protein in cyanobacteria. Molecular Microbiology, Volume 94 (Number 5). pp. 1179-1195. doi:10.1111/mmi.12826

[img]
Preview
PDF (Creative Commons : Attribution 4.0)
WRAP_mmi12826.pdf - Published Version - Requires a PDF viewer.

Download (24Mb) | Preview
Official URL: http://dx.doi.org/10.1111/mmi.12826

Request Changes to record.

Abstract

The Vipp1 protein is essential in cyanobacteria and chloroplasts for the maintenance of photosynthetic function and thylakoid membrane architecture. To investigate its mode of action we generated strains of the cyanobacteria Synechocystis sp. PCC6803 and Synechococcus sp. PCC7942 in which Vipp1 was tagged with green fluorescent protein at the C-terminus and expressed from the native chromosomal locus. There was little perturbation of function. Live-cell fluorescence imaging shows dramatic relocalisation of Vipp1 under high light. Under low light, Vipp1 is predominantly dispersed in the cytoplasm with occasional concentrations at the outer periphery of the thylakoid membranes. High light induces Vipp1 coalescence into localised puncta within minutes, with net relocation of Vipp1 to the vicinity of the cytoplasmic membrane and the thylakoid membranes. Pull-downs and mass spectrometry identify an extensive collection of proteins that are directly or indirectly associated with Vipp1 only after high-light exposure. These include not only photosynthetic and stress-related proteins but also RNA-processing, translation and protein assembly factors. This suggests that the Vipp1 puncta could be involved in protein assembly. One possibility is that Vipp1 is involved in the formation of stress-induced localised protein assembly centres, enabling enhanced protein synthesis and delivery to membranes under stress conditions.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
Divisions: Faculty of Science > Mathematics
Library of Congress Subject Headings (LCSH): Cyanobacteria -- Physiology, Bacterial proteins
Journal or Publication Title: Molecular Microbiology
Publisher: Wiley-Blackwell Publishing Ltd.
ISSN: 0950-382X
Official Date: 26 November 2014
Dates:
DateEvent
26 November 2014Published
30 October 2014Available
9 October 2014Accepted
Date of first compliant deposit: 28 December 2015
Volume: Volume 94
Number: Number 5
Page Range: pp. 1179-1195
DOI: 10.1111/mmi.12826
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Seventh Framework Programme (European Commission) (FP7), European Commission (EC), Oxford Centre for Integrative Systems Biology, Royal Society (Great Britain), Engineering and Physical Sciences Research Council (EPSRC)
Grant number: BB/G021856 (BBSRC), FOR 929 (DFG), SCHN 690/3-1 (DFG), FP7- PEOPLE-2009-IEF 254575 (FP7), NFR 192436 (EC), 197119 (EC), EP/G0061009/1 (EPSRC)

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