Differential Proteomics Based on Multidimensional Protein Identification Technology to Understand the Biogenesis of Outer Membrane of Escherichia coli

2016 ◽  
pp. 57-70 ◽  
Author(s):  
Alessandra M. Martorana ◽  
Sara Motta ◽  
Paola Sperandeo ◽  
Pierluigi Mauri ◽  
Alessandra Polissi
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Protein Identification ◽  
Differential Proteomics ◽  
Multidimensional Protein Identification Technology

scholarly journals Effects of SecE Depletion on the Inner and Outer Membrane Proteomes of Escherichia coli

2008 ◽  
Vol 190 (10) ◽  
pp. 3505-3525 ◽  
Author(s):  
Louise Baars ◽  
Samuel Wagner ◽  
David Wickström ◽  
Mirjam Klepsch ◽  
A. Jimmy Ytterberg ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Protein Identification ◽  
Protein Translocation ◽  
Outer Membrane Proteins ◽  
Specific Model ◽  
Secretory Proteins ◽  
Inner Membrane ◽  
Sec Translocon

ABSTRACT The Sec translocon is a protein-conducting channel that allows polypeptides to be transferred across or integrated into a membrane. Although protein translocation and insertion in Escherichia coli have been studied using only a small set of specific model substrates, it is generally assumed that most secretory proteins and inner membrane proteins use the Sec translocon. Therefore, we have studied the role of the Sec translocon using subproteome analysis of cells depleted of the essential translocon component SecE. The steady-state proteomes and the proteome dynamics were evaluated using one- and two-dimensional gel analysis, followed by mass spectrometry-based protein identification and extensive immunoblotting. The analysis showed that upon SecE depletion (i) secretory proteins aggregated in the cytoplasm and the cytoplasmic σ32 stress response was induced, (ii) the accumulation of outer membrane proteins was reduced, with the exception of OmpA, Pal, and FadL, and (iii) the accumulation of a surprisingly large number of inner membrane proteins appeared to be unaffected or increased. These proteins lacked large translocated domains and/or consisted of only one or two transmembrane segments. Our study suggests that several secretory and inner membrane proteins can use Sec translocon-independent pathways or have superior access to the remaining Sec translocons present in SecE-depleted cells.

scholarly journals Dissecting Escherichia coli Outer Membrane Biogenesis Using Differential Proteomics

PLoS ONE ◽  
2014 ◽  
Vol 9 (6) ◽  
pp. e100941 ◽  
Author(s):  
Alessandra M. Martorana ◽  
Sara Motta ◽  
Dario Di Silvestre ◽  
Federica Falchi ◽  
Gianni Dehò ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Membrane Biogenesis ◽  
Differential Proteomics ◽  
Outer Membrane Biogenesis

Overexpression of Outer Membrane Protein A Is a Risk Factor for Mortality in Escherichia coli Bloodstream Infections

2019 ◽  
Author(s):  
Ángel Rodríguez-Villodres ◽  
Rocío Álvarez-Marín ◽  
María Antonia Pérez-Moreno ◽  
Andrea Miró-Canturri ◽  
Marco Durán Lobato ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Risk Factor ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Bloodstream Infections ◽  
Outer Membrane Protein A

Preparation of Outer Membrane Vesicle from Escherichia coli

BIO-PROTOCOL ◽  
2013 ◽  
Vol 3 (23) ◽  
Author(s):  
Oh Kim ◽  
Bok Hong ◽  
Kyong-Su Park ◽  
Yae Yoon ◽  
Seng Choi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Membrane Vesicle ◽  
Outer Membrane Vesicle
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