Increases in Acidic Phospholipid Contents Specifically Restore Protein Translocation in a Cold-sensitive secA orsecG Null Mutant

Suzuki, Hirofumi; Nishiyama, Kenichi; Tokuda, Harukuni

doi:10.1074/jbc.274.43.31020

Cited by 22 publications

(34 citation statements)

References 48 publications

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“…Of the bilayer constituents, the response seems to be specific to CL and to a lesser degree PG. The results explain a number of observations specifying the requirement of acidic phospholipids in protein translocation (1)(2)(3)(4)(5)23). The inherent symmetry of CL, with two glycerol-linked PGs, might be utilized in the interaction with twin copies of SecYEG.…”

Section: Discussionsupporting

confidence: 67%

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The action of cardiolipin on the bacterial translocon

Gold

Robson

Bao

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

150

153

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Cardiolipin is an ever-present component of the energy-conserving inner membranes of bacteria and mitochondria. Its modulation of the structure and dynamism of the bilayer impacts on the activity of their resident proteins, as a number of studies have shown. Here we analyze the consequences cardiolipin has on the conformation, activity, and localization of the protein translocation machinery. Cardiolipin tightly associates with the SecYEG protein channel complex, whereupon it stabilizes the dimer, creates a high-affinity binding surface for the SecA ATPase, and stimulates ATP hydrolysis. In addition to the effects on the structure and function, the subcellular distribution of the complex is modified by the cardiolipin content of the membrane. Together, the results provide rare and comprehensive insights into the action of a phospholipid on an essential transport complex, which appears to be relevant to a broad range of energy-dependent reactions occurring at membranes.

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Section: Discussionsupporting

confidence: 67%

“…In keeping with this, the bacterial protein translocation reaction, driven by the ATPase SecA through the conserved SecYEG complex, has a known requirement for acidic phospholipids (1)(2)(3)(4)(5).…”

mentioning

confidence: 99%

The action of cardiolipin on the bacterial translocon

Gold

Robson

Bao

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

150

153

View full text Add to dashboard Cite

show abstract

mentioning

confidence: 86%

“…Likewise, the cold-sensitive growth defect of the secAcsR11 mutant strain is suppressed by overproduction of the PgsA protein (28). These effects have been attributed to an increase in the anionic phospholipid content that restores the secretion defect of these strains by facilitating the SecA catalytic cycle at low temperature (28). The exact mechanism of this activation, however, remains obscure as studies with photoreactive phospholipid analogues suggest that the SecYEG-bound, membrane-inserted form of SecA is not in contact with phospholipids (29,30).…”

mentioning

confidence: 99%

Non-bilayer Lipids Stimulate the Activity of the Reconstituted Bacterial Protein Translocase

Does

Swaving

Klompenburg

et al. 2000

Journal of Biological Chemistry

115

100

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To determine the phospholipid requirement of the preprotein translocase in vitro, the Escherichia coli SecYEG complex was purified in a delipidated form using the detergent dodecyl maltoside. SecYEG was reconstituted into liposomes composed of defined synthetic phospholipids, and proteoliposomes were analyzed for their preprotein translocation and SecA translocation ATPase activity. The activity strictly required the presence of anionic phospholipids, whereas the non-bilayer lipid phosphatidylethanolamine was found stimulatory. The latter effect could also be induced by dioleoylglycerol, a lipid that adopts a non-bilayer conformation. Phosphatidylethanolamine derivatives that prefer the bilayer state were unable to stimulate translocation. In the absence of SecG, activity was reduced, but the phospholipid requirement was unaltered. Remarkably, nonbilayer lipids were found essential for the activity of the Bacillus subtilis SecYEG complex. Optimal activity required a mixture of anionic and non-bilayer lipids at concentrations that correspond to concentrations found in the natural membrane.

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“…This defect could be relieved by increasing the anionic lipid content of the membrane [42,43]. Since SecG has been reported to change its topology upon SecA interaction and thereby possibly stimulates SecA activity [44,45], the SecG deletion defect is probably restored by lipid effects via SecA.…”

Section: Influences Of Pgmentioning

confidence: 99%

The role of lipids in membrane insertion and translocation of bacterial proteins

VANDALEN

2004

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Phospholipids are essential building blocks of membranes and maintain the membrane permeability barrier of cells and organelles. They provide not only the bilayer matrix in which the functional membrane proteins reside, but they also can play direct roles in many essential cellular processes. In this review, we give an overview of the lipid involvement in protein translocation across and insertion into the Escherichia coli inner membrane. We describe the key and general roles that lipids play in these processes in conjunction with the protein components involved. We focus on the Sec-mediated insertion of leader peptidase. We describe as well the more direct roles that lipids play in insertion of the small coat proteins Pf3 and M13. Finally, we focus on the role of lipids in membrane assembly of oligomeric membrane proteins, using the potassium channel KcsA as model protein. In all cases, the anionic lipids and lipids with small headgroups play important roles in either determining the efficiency of the insertion and assembly process or contributing to the directionality of the insertion process. D

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Increases in Acidic Phospholipid Contents Specifically Restore Protein Translocation in a Cold-sensitive secA orsecG Null Mutant

Cited by 22 publications

References 48 publications

The action of cardiolipin on the bacterial translocon

The action of cardiolipin on the bacterial translocon

Non-bilayer Lipids Stimulate the Activity of the Reconstituted Bacterial Protein Translocase

The role of lipids in membrane insertion and translocation of bacterial proteins

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