TY - JOUR
T1 - Consequences of depletion of the signal recognition particle in Escherichia coli
AU - Wickstrom, D.
AU - Wagner, S.
AU - Baars, L
AU - Ytterberg, A.J.
AU - Klepsch, M.
AU - van Wijk, K.J.
AU - Luirink, J.
AU - de Gier, J.W.
N1 - 1083-351x Wickstrom, David Wagner, Samuel Baars, Louise Ytterberg, A Jimmy Klepsch, Mirjam van Wijk, Klaas J Luirink, Joen de Gier, Jan-Willem 5R01GM081827-03/GM/NIGMS NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't United States J Biol Chem. 2011 Feb 11;286(6):4598-609. doi: 10.1074/jbc.M109.081935. Epub 2010 Oct 5.
PY - 2011
Y1 - 2011
N2 - Thus far, the role of the Escherichia coli signal recognition particle (SRP) has only been studied using targeted approaches. It has been shown for a handful of cytoplasmic membrane proteins that their insertion into the cytoplasmic membrane is at least partially SRP-dependent. Furthermore, it has been proposed that the SRP plays a role in preventing toxic accumulation of mistargeted cytoplasmic membrane proteins in the cytoplasm. To complement the targeted studies on SRP, we have studied the consequences of the depletion of the SRP component Fifty-four homologue (Ffh) in E. coli using a global approach. The steady-state proteomes and the proteome dynamics were evaluated using oneand two-dimensional gel analysis, followed by mass spectrometry-based protein identification and immunoblotting. Our analysis showed that depletion of Ffh led to the following: (i) impaired kinetics of the biogenesis of the cytoplasmic membrane proteome; (ii) lowered steady-state levels of the respiratory complexes NADH dehydrogenase, succinate dehydrogenase, and cytochrome bo
AB - Thus far, the role of the Escherichia coli signal recognition particle (SRP) has only been studied using targeted approaches. It has been shown for a handful of cytoplasmic membrane proteins that their insertion into the cytoplasmic membrane is at least partially SRP-dependent. Furthermore, it has been proposed that the SRP plays a role in preventing toxic accumulation of mistargeted cytoplasmic membrane proteins in the cytoplasm. To complement the targeted studies on SRP, we have studied the consequences of the depletion of the SRP component Fifty-four homologue (Ffh) in E. coli using a global approach. The steady-state proteomes and the proteome dynamics were evaluated using oneand two-dimensional gel analysis, followed by mass spectrometry-based protein identification and immunoblotting. Our analysis showed that depletion of Ffh led to the following: (i) impaired kinetics of the biogenesis of the cytoplasmic membrane proteome; (ii) lowered steady-state levels of the respiratory complexes NADH dehydrogenase, succinate dehydrogenase, and cytochrome bo
UR - https://www.scopus.com/pages/publications/79953009533
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U2 - 10.1074/jbc.M109.081935
DO - 10.1074/jbc.M109.081935
M3 - Article
SN - 0021-9258
VL - 286
SP - 4598
EP - 4609
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 286
ER -