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

Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores

Tools
- Tools
+ Tools

Beck, Daniel, Vasisht, Nishi, Baglieri, J., Monteferrante, Carmine G., Dijl, Jan Maarten van, Robinson, Colin and Smith, Corinne J. (2013) Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Volume 1833 (Number 8). pp. 1811-1819. doi:10.1016/j.bbamcr.2013.03.028 ISSN 0167-4889.

[img]
Preview
Text
WRAP_Smith_0170774-lf-170413-bbamcr-13-58r1_revised_and_submitted_forwrap.pdf - Accepted Version

Download (3371Kb) | Preview
Official URL: http://dx.doi.org/10.1016/j.bbamcr.2013.03.028

Request Changes to record.

Abstract

Tat-dependent protein transport permits the traffic of fully folded proteins across membranes in bacteria and chloroplasts. The mechanism by which this occurs is not understood. Current theories propose that a key step requires the coalescence of a substrate-binding TatC-containing complex with a TatA complex, which forms pores of varying sizes that could accommodate different substrates. We have studied the structure of the TatAd complex from Bacillus subtilis using electron microscopy to generate the first 3D model of a TatA complex from a Gram-positive bacterium. We observe that TatAd does not exhibit the remarkable heterogeneity of Escherichia coli TatA complexes but instead forms ring-shaped complexes of 7.5–9 nm diameter with potential pores of 2.5–3 nm diameter that are occluded at one end. Such structures are consistent with those seen for E. coli TatE complexes. Furthermore, the small diameter of the TatAd pore, and the homogeneous nature of the complexes, suggest that TatAd cannot form the translocation channel by itself. Biochemical data indicate that another B. subtilis TatA complex, TatAc, has similar properties, suggesting a common theme for TatA-type complexes from Bacillus.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher: Elsevier BV
ISSN: 0167-4889
Official Date: 2013
Dates:
DateEvent
2013Published
Volume: Volume 1833
Number: Number 8
Page Range: pp. 1811-1819
DOI: 10.1016/j.bbamcr.2013.03.028
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Date of first compliant deposit: 24 December 2015
Date of first compliant Open Access: 24 December 2015

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