Consequences of the interaction of calcium with dioleoylphosphatidate-containing model membranes: calcium-membrane and membrane-membrane interactions

Smaal, Erik B.; Mandersloot, J.G.; Demel, R.A.; Kruijff, Ben de; Gier, J. De

doi:10.1016/0005-2736(87)90326-9

Cited by 36 publications

(18 citation statements)

References 34 publications

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“…In this scenario it may not be of major importance whether calcium is primarily bound at the enzyme or at the surface of the membrane phospholipids. Biomembranes and phospholipid vesicles are capable of binding calcium via ionic interactions with their negatively charged phosphate groups (30,31). For dioleoylphosphatidate/dioleoylphosphatidylcholine multilamellar vesicles (2:8 mol %) calcium was shown to neutralize these negative charges on the liposome surface and thus, induces vesicle fusion and aggregation (44).…”

Section: Discussionmentioning

confidence: 99%

“…However, it remained unclear whether calcium primarily binds to the LOX, to the membranes, or to both. It is well known that biomembranes effectively bind calcium via electrostatic interactions with negatively charged phospholipid head groups (30,31). In fact, most biomembrane preparations contain large amounts of calcium when prepared in the absence of EDTA.…”

Section: Identification Of Novel Sequence Determinants Involved Inmentioning

confidence: 99%

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Investigations into Calcium-dependent Membrane Association of 15-Lipoxygenase-1

Walther

Wiesner

Kühn

2004

Journal of Biological Chemistry

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Taken together these data suggest that 15-lipoxygenase-1 associates to biomembranes primarily via hydrophobic interactions between surface-exposed apolar amino acid side chains and membrane lipids. Calcium supports membrane binding probably by forming salt bridges between the negatively charged head groups of membrane phospholipids and acidic surface amino acids of the membrane contact plane and this interaction might contribute to overcome repulsive forces.

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Section: Discussionmentioning

confidence: 99%

Section: Identification Of Novel Sequence Determinants Involved Inmentioning

confidence: 99%

Investigations into Calcium-dependent Membrane Association of 15-Lipoxygenase-1

Walther

Wiesner

Kühn

2004

Journal of Biological Chemistry

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“…In monolayer experiments both binding and insertion are reduced albeit to a different extent by nucleotides (35). Because the relation between the molecular area and surface pressure is known for DOPG monolayers (54), it is possible to estimate the molecular area of SecA for different lipid-bound conformations. The molecular area in the presence of ATP is approximately 1.5 times more as compared to the situation without nucleotides (or with nonhydrolyzable nucleotides) from ∼5 to ∼8 nm 2 , respectively.…”

Section: Discussionmentioning

confidence: 99%

Translocase-Bound SecA Is Largely Shielded from the Phospholipid Acyl Chains

et al. 1998

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Protein translocation in Escherichia coli is mediated by the SecA ATPase bound to the SecYEG membrane protein complex. SecA translocation ATPase activity as well as protein translocation is dependent on the presence of negatively charged lipids. By using a phospholipid with an acyl chain linked photoactivatable group, the lipid accessibility of SecA bound at the translocase was explored. SecA bound to lipid vesicles containing negatively charged lipids was found to be readily accessible for labeling by the photoactivatable phospholipid. The presence of an excess amount of SecYEG complex resulted in a remarkable reduction in the amount of lipid-accessible SecA irrespective of the nucleotide-bound form of SecA. These data demonstrate that the SecYEG-bound SecA is largely shielded from the phospholipid acyl chains and suggest the presence of two distinct pools of membrane-bound SecA that differ in the degree of lipid association.

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“…This demonstrates that prefd is differently inserted into MGDG and DOPG monolayers. Using the ~r-A characteristics of DOPG [28] and MGDG [29] it was calculated that an inserted prefd molecule…”

Section: 0"mentioning

confidence: 99%