On the possible participation of acid phospholipids in the translocation of secreted proteins through the bacterial cytoplasmic membrane

Nesmeyanova, M. A.

doi:10.1016/0014-5793(82)80131-2

Cited by 76 publications

(41 citation statements)

References 44 publications

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“…This last inhibition by duramycin could be completely reversed by phospholipids. The inhibition of protein translocation by duramycin ( (11,21) and is consistent with the experimental evidence that a synthetic'signal peptide spontaneously inserts into the lipid monolatyer and undergoes certain conformational change (2,3). The signal peptide also inhibits the ATP-dependent protein translocation into membrane vesicles, either by competing for a receptor or by affecting lipid bilayers (8).…”

Section: Discussionsupporting

confidence: 61%

Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles

Tai¹

1987

J Bacteriol

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The effects of several membrane antibiotics and other agents on ATP-dependent protein translocation were examined in membrane vesicles under conditions where no significant proton motive force was present. The membrane perturbants ethanol and procaine abolished ATP-dependent protein translocation. Phenethyl alcohol at low concentrations abolished translocation, whereas at high concentrations it allowed precursors to be translocated but inhibited their processing. Translocation of precursors promoted by phenethyl alcohol was temperature dependent and occurred without an added energy source but was enhanced by ATP. However, such precursors could not be further processed to mature forms upon removal of the alcohol. The membrane-active antibiotics polymyxin B and gramicidin S were strong inhibitors of translocation, whereas gramicidin D, cerulenin, and mycobacillin had no effect even at higher concentrations, indicating some specificity in interference with protein translocation. Duramycin, an antibiotic previously shown to affect protein-lipid interaction, severely impaired protein translocation. These results showed that membrane structures play important roles, either directly or indirectly, in protein translocation. Chelating agents

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Section: Discussionsupporting

confidence: 61%

Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles

Tai¹

1987

J Bacteriol

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“…salicarius membrane lipids with unsaturated fatty acids, and the assumed attendant increase in membrane fluidity (Kimura & Izui, 1976;Cronan & Gelmann, 1975;Evkokimova et a/., 1978;Nesmeyanova, 1982), is not the sole requirement for maximum production of extracellular glucosyltransferase. Cells grown at 30 "C without Tween 80 had a U/S ratio (2.06) greater than cells grown at 37 "C or 40 "C with the detergent (1.65 and 1.42; Table 3), yet produced only about one-tenth as much extracellular glucosyltransferase (Table 4).…”

Section: Discussionmentioning

confidence: 99%

Does an Increase in Membrane Unsaturated Fatty Acids Account for Tween 80 Stimulation of Glucosyltransferase Secretion by Streptococcus salivarius?

Jacques¹,

Jacques²,

Wolf³

et al. 1985

Microbiology

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“…However, recent studies showed the existence of a close link between the secretory process and composition, turnover and physicochemical state of membrane phospholipids (16)(17)(18), and a number of hypotheses of molecular mechanism of involvement of these compounds in the secretory process were proposed (16)(17)(18)(19). The fact that, besides the signal peptide, relatively small molecules of phospholipids play an important role in the process of translocation, opened a principal possibility for the elucidation of the molecular mechanism of translocation by the theoretical methods of structural analysis.…”

Section: Kajava Eta/mentioning

confidence: 99%

Stereochemical Analysis of Interaction of Signal Peptide with Phospholipids at the Initiation of Protein Translocation Across the Membrane

Kajava

Bogdanov

Nesmeyanova

1991

Journal of Biomolecular Structure and Dynamics

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Stereochemical analysis of signal peptide interaction with E. coli membrane phospholipids revealed the structural complementarity of N-terminus of signal peptide alpha-helix and acid phospholipids. The formation of their complex leads to neutralization of charges and decrease in hydrophilicity of both components, and promotes insertion of peptide and phospholipid into the membrane, not separately but as a complex. Interaction of acid phospholipids with the E. coli alkaline phosphatase (AP) signal peptide was thoroughly analyzed, and it was shown that in this case a complex of signal peptide alpha-helix with phosphatidylglycerol is inserted into the membrane with the lowest energy expense. On the basis of the results of stereochemical analysis and the available experimental data, a molecular mechanism of protein translocation initiation across the membrane has been proposed, in which the key events are the formation of the complex "signal peptide alpha-helix-acid phospholipid", the coupled insertion of hydrophobic peptide-lipid complex into a nonpolar membrane interior and translocation across the membranes.

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On the possible participation of acid phospholipids in the translocation of secreted proteins through the bacterial cytoplasmic membrane

Cited by 76 publications

References 44 publications

Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles

Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles

Does an Increase in Membrane Unsaturated Fatty Acids Account for Tween 80 Stimulation of Glucosyltransferase Secretion by Streptococcus salivarius?

Stereochemical Analysis of Interaction of Signal Peptide with Phospholipids at the Initiation of Protein Translocation Across the Membrane

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