The University of Southampton
University of Southampton Institutional Repository

Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part I: the effect of growth temperature

Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part I: the effect of growth temperature
Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part I: the effect of growth temperature
The response of the cold-adapted (psychrophilic) methanogenic archaeon Methanococcoides burtonii to growth temperature was investigated using differential proteomics (postincorporation isobaric labeling) and tandem liquid chromatography-mass spectrometry (LC/LC-MS/MS). This is the first proteomic study of M. burtonii to include techniques that specifically enrich for both surface and membrane proteins and to assess the effects of growth temperature (4 vs 23 degrees C) and carbon source (trimethylamine vs methanol) on cellular protein levels. Numerous surface layer proteins were more abundant at 4 degrees C, indicating an extensive remodeling of the cell envelope in response to low temperature. Many of these surface proteins contain domains associated with cell adhesion. Within the cell, small proteins each composed of a single TRAM domain were recovered as important cold adaptation proteins and might serve as RNA chaperones, in an analogous manner to Csp proteins (absent from M. burtonii). Other proteins that had higher abundances at 4 degrees C can be similarly tied to relieving or resolving the adverse affects of cold growth temperature on translational capacity and correct protein folding. The proteome of M. burtonii grown at 23 degrees C was dominated by oxidative stress proteins, as well as a large number of integral membrane proteins of unknown function. This is the first truly global proteomic study of a psychrophilic archaeon and greatly expands knowledge of the cellular mechanisms underpinning cold adaptation in the Archaea.
1535-3893
640-652
Williams, Timothy J.
c45d1f23-12f3-4dab-bebb-e89fb7219e26
Burg, Dominic W.
a51bc2a5-54d3-40ee-ac66-4ca0bc4d9d1d
Raftery, Mark J.
6050a0f6-677d-468d-ac46-76663d1ac6c3
Poljak, Anne
114fe1b4-3275-4d81-8d9c-ff523cd18254
Guilhaus, Michael
f2e34a05-c65c-41cc-9f30-268d41d5d3e7
Pilak, Oliver
b7025bf7-7e05-4194-8aae-67b26f977a6f
Cavicchioli, Ricardo
95c04c14-6cdd-4f0d-afc6-32bdbfa53ad9
Williams, Timothy J.
c45d1f23-12f3-4dab-bebb-e89fb7219e26
Burg, Dominic W.
a51bc2a5-54d3-40ee-ac66-4ca0bc4d9d1d
Raftery, Mark J.
6050a0f6-677d-468d-ac46-76663d1ac6c3
Poljak, Anne
114fe1b4-3275-4d81-8d9c-ff523cd18254
Guilhaus, Michael
f2e34a05-c65c-41cc-9f30-268d41d5d3e7
Pilak, Oliver
b7025bf7-7e05-4194-8aae-67b26f977a6f
Cavicchioli, Ricardo
95c04c14-6cdd-4f0d-afc6-32bdbfa53ad9

Williams, Timothy J., Burg, Dominic W., Raftery, Mark J., Poljak, Anne, Guilhaus, Michael, Pilak, Oliver and Cavicchioli, Ricardo (2010) Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part I: the effect of growth temperature. Journal of Proteome Research, 9 (2), 640-652. (doi:10.1021/pr900509n). (PMID:20039705)

Record type: Article

Abstract

The response of the cold-adapted (psychrophilic) methanogenic archaeon Methanococcoides burtonii to growth temperature was investigated using differential proteomics (postincorporation isobaric labeling) and tandem liquid chromatography-mass spectrometry (LC/LC-MS/MS). This is the first proteomic study of M. burtonii to include techniques that specifically enrich for both surface and membrane proteins and to assess the effects of growth temperature (4 vs 23 degrees C) and carbon source (trimethylamine vs methanol) on cellular protein levels. Numerous surface layer proteins were more abundant at 4 degrees C, indicating an extensive remodeling of the cell envelope in response to low temperature. Many of these surface proteins contain domains associated with cell adhesion. Within the cell, small proteins each composed of a single TRAM domain were recovered as important cold adaptation proteins and might serve as RNA chaperones, in an analogous manner to Csp proteins (absent from M. burtonii). Other proteins that had higher abundances at 4 degrees C can be similarly tied to relieving or resolving the adverse affects of cold growth temperature on translational capacity and correct protein folding. The proteome of M. burtonii grown at 23 degrees C was dominated by oxidative stress proteins, as well as a large number of integral membrane proteins of unknown function. This is the first truly global proteomic study of a psychrophilic archaeon and greatly expands knowledge of the cellular mechanisms underpinning cold adaptation in the Archaea.

This record has no associated files available for download.

More information

e-pub ahead of print date: 1 December 2009
Published date: 5 February 2010
Organisations: Molecular and Cellular

Identifiers

Local EPrints ID: 338909
URI: http://eprints.soton.ac.uk/id/eprint/338909
ISSN: 1535-3893
PURE UUID: 78e63867-640d-4db5-89d2-ccfca835bec0

Catalogue record

Date deposited: 18 May 2012 13:25
Last modified: 14 Mar 2024 11:06

Export record

Altmetrics

Contributors

Author: Timothy J. Williams
Author: Dominic W. Burg
Author: Mark J. Raftery
Author: Anne Poljak
Author: Michael Guilhaus
Author: Oliver Pilak
Author: Ricardo Cavicchioli

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×