Title : Ionic Hydrogen Bonds and Lipid Packing Defects Determine the Binding Orientation and Insertion Depth of RecA on Multicomponent Lipid Bilayers.

Pub. Date : 2016 Aug 25

PMID : 27095675






8 Functional Relationships(s)
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1 Fluorescence measurements indicate that RecA behaves differently when bound to phosphatidylglycerol (PG)- and cardiolipin (CL)-containing liposomes. Phosphatidylglycerols RAD51 recombinase Homo sapiens
2 Fluorescence measurements indicate that RecA behaves differently when bound to phosphatidylglycerol (PG)- and cardiolipin (CL)-containing liposomes. Phosphatidylglycerols RAD51 recombinase Homo sapiens
3 Ionic hydrogen bonds between the carboxylate group in phosphatidylserine and several lysine residues in the C-terminal region of RecA stabilize the parallel ( ) binding orientation, which is not locally stable on PG- and CL-containing membranes despite similarity in the overall charge density. Phosphatidylglycerols RAD51 recombinase Homo sapiens
4 The computational finding that RecA binds in a similar orientation to PG- and CL-containing membranes is consistent with the fact that PG alone is sufficient to induce RecA polar localization, although CL might be more effective because of its tighter binding to RecA. Phosphatidylglycerols RAD51 recombinase Homo sapiens
5 The computational finding that RecA binds in a similar orientation to PG- and CL-containing membranes is consistent with the fact that PG alone is sufficient to induce RecA polar localization, although CL might be more effective because of its tighter binding to RecA. Phosphatidylglycerols RAD51 recombinase Homo sapiens
6 The computational finding that RecA binds in a similar orientation to PG- and CL-containing membranes is consistent with the fact that PG alone is sufficient to induce RecA polar localization, although CL might be more effective because of its tighter binding to RecA. Phosphatidylglycerols RAD51 recombinase Homo sapiens
7 The different fluorescence behaviors of RecA upon binding to PG- and CL-containing liposomes is likely due to the different structures and flexibility of the C-terminal region of RecA when it binds to different anionic phospholipids. Phosphatidylglycerols RAD51 recombinase Homo sapiens
8 The different fluorescence behaviors of RecA upon binding to PG- and CL-containing liposomes is likely due to the different structures and flexibility of the C-terminal region of RecA when it binds to different anionic phospholipids. Phosphatidylglycerols RAD51 recombinase Homo sapiens