First complexomic study of alkane-binding protein complexes in the yeast Yarrowia lipolytica
Talanta. 2010-02-15; 80(4): 1576-1585
DOI: 10.1016/j.talanta.2009.07.016
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1. Talanta. 2010 Feb 15;80(4):1576-85. doi: 10.1016/j.talanta.2009.07.016. Epub 2009
Jul 10.
First complexomic study of alkane-binding protein complexes in the yeast Yarrowia
lipolytica.
Lasserre JP(1), Nicaud JM, Pagot Y, Joubert-Caron R, Caron M, Hardouin J.
Author information:
(1)Laboratoire de Biochimie des Protéines et Protéomique, UMR CNRS 7033,
Université Paris 13, 74 rue Marcel Cachin, F-93017 Bobigny cedex, France.
The yeast Yarrowia lipolytica uses hydrophobic substrates, such as alkanes, fatty
acids and oils, for its growth. It has developed a strategy for the use of such
substrates, involving the production of hydrophobic binding structures called
protrusions on the cell surface. These protrusions are resemble channels
connecting the cell wall to the inside of the cell, and are probably involved in
transport mechanisms that we do not yet fully understand. The complete genome of
the haploid Y. lipolytica strain E150 (CLIB99) was sequenced in 2004 by the
Génolevures Consortium. The availability of a complete genome sequence for this
species has made it possible to carry out proteomic and other investigations,
leading to the characterization of lipid bodies (LB) in terms of (i) their lipid
composition, (ii) the major LB proteins, as identified by mass spectrometry, and
(iii) differences in protein or lipid composition as a function of the carbon
source used. Functional analyses would provide insight into the biological
processes associated with these bodies and 2D BN/SDS-PAGE is a highly suitable
method for the analysis of protein complexes. This report provides a first
description of the analysis and identification of hydrophobic binding protein
complexes in Y. lipolytica. For this purpose, we used 2D BN/SDS-PAGE for the
separation of protein complexes and HPLC-chip-MS for protein identification. We
separated and identified 40 protein complexes (11 heteromultimeric and 29
homomultimeric), providing insight into their function. This study represents a
major step forward, as most previous studies identified proteins either on the
basis of sequence similarity to proteins from other organisms (44% of the
proteins identified in this study) or by prediction (50% of proteins identified
in this study) alone.
(c) 2009 Elsevier B.V. All rights reserved.
DOI: 10.1016/j.talanta.2009.07.016
PMID: 20082817 [Indexed for MEDLINE]