Morin Isabelle, Cuillel Martine, Lowe Jennifer, Crouzy Serge, Guillain Florent, Mintz Elisabeth
Laboratoire de Biophysique Moléculaire et Cellulaire, UMR 5090 CEA-CNRS-Université Joseph Fourier, CEA/DRDC/BMC, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France.
FEBS Lett. 2005 Feb 14;579(5):1117-23. doi: 10.1016/j.febslet.2005.01.008.
Copper delivery to Ccc2--the Golgi Cu+-ATPase--was investigated in vivo, replacing the Cu+-chaperone Atx1 by various structural homologues in an atx1-Delta yeast strain. Various proteins, displaying the same ferredoxin-like fold and (M/L)(T/S)CXXC metal-binding motif as Atx1 and known as Cu+-, Cd2+- or Hg2+-binding proteins were able to replace Atx1. Therefore, regardless of their original function, these proteins could all bind copper and transfer it to Ccc2, suggesting that Ccc2 is opportunistic and can interact with many different proteins to gain Cu+. The possible role of electrostatic potential surfaces in the docking of Ccc2 with these Atx1-homologues is discussed.
在体内研究了铜向高尔基体铜离子 - ATP酶Ccc2的传递情况，在atx1 - Δ酵母菌株中用各种结构同源物替代铜离子伴侣Atx1。各种蛋白质，与Atx1具有相同的铁氧化还原蛋白样折叠以及（M/L）（T/S）CXXC金属结合基序，并且已知为铜离子、镉离子或汞离子结合蛋白，都能够替代Atx1。因此，无论其原始功能如何，这些蛋白质都能结合铜并将其传递给Ccc2，这表明Ccc2具有机会性，能够与许多不同蛋白质相互作用以获取铜离子。文中讨论了静电势表面在Ccc2与这些Atx1同源物对接中的可能作用。
