Enzymatic cross-linking of purple membranes catalyzed by bacterial transglutaminase.
Enzymatic cross-linking of purple membranes catalyzed by bacterial transglutaminase.
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DOI：
10.1021/bm0056207
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发表时间：
2001
影响因子：
6.2
通讯作者：
A. Seitz;F. Schneider;R. Pasternack;H. Fuchsbauer;N. Hampp
中科院分区：
文献类型：
--
作者：
A. Seitz;F. Schneider;R. Pasternack;H. Fuchsbauer;N. Hampp
研究发现，细菌转谷氨酰胺酶（TGase）在温和条件下促进紫膜（PM）形式的细菌视紫红质（BR）的选择性交联。使用荧光探针检测膜蛋白 BR 可能充当谷氨酰胺供体以及 TGase 的赖氨酸供体。结合位点被确定为 Gln-3 作为反应性谷氨酰胺，Lys-129 是相应的赖氨酸残基。将 PM 与 TGase 一起孵育后，无需额外的间隔分子即可实现 PM 贴片的交联。据我们所知，这是首次报道膜结合蛋白的膜间交联。此外，这一发现可能提供实现完整紫色膜片与合成聚合物共价连接的能力。
It was found that bacterial transglutaminase (TGase) facilitates selective cross-linking of bacteriorhodopsin (BR) in purple membrane (PM) form under mild conditions. Fluorescent probes were used to detect that the membrane protein BR may act as a glutamine donor as well as a lysine donor for TGase. The binding sites were determined to be Gln-3 as the reactive glutamine, and Lys-129 is the corresponding lysine residue. Upon incubation of PM with TGase, cross-linking of PM patches can be achieved without an additional spacer molecule. To our knowledge, this is the first time that an intermembrane cross-linking of membrane-bound proteins is reported. Furthermore, this finding may provide the ability to achieve covalent linkage of complete purple membrane patches to synthetic polymers.