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In cells a portion of cytochrome c (cyt c) (15–20%) is tightly bound to cardiolipin (CL), one of the phospholipids constituting the mitochondrial membrane. The CL-bound protein, which has nonnative tertiary structure, altered heme pocket, and disrupted Fe(III)-M80 axial bond, is thought to play a role in the apoptotic process. This has attracted considerable interest in order to clarify the mechanisms governing the cyt c–CL interaction. Herein we have investigated the binding reaction of CL with the c-type cytochromes from horse heart and yeast. Although the two proteins possess a similar tertiary architecture, yeast cyt c displays lower stability and, contrary to the equine protein, it does not bind ATP and lacks pro-apoptotic activity. The study has been performed in the absence and in the presence of ATP and NaCl, two compounds that influence the (horse cyt c)-CL binding process and, thus, the pro-apoptotic activity of the protein. The two proteins behave differently: while CL interaction with horse cyt c is strongly influenced by the two effectors, no effect is observed for yeast cyt c. It is noteworthy that NaCl induces dissociation of the (horse cyt c)–CL complex but has no influence on that of yeast cyt c. The differences found for the two proteins highlight that specific structural factors, such as the different local structure conformation of the regions involved in the interactions with either CL or ATP, can significantly affect the behavior of cyt c in its reaction with liposomes and the subsequent pro-apoptotic action of the protein.

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放手-心淡: 金幣+20, ★★★很有幫助, 謝謝你 2015-07-08 01:22:37

細(xì)胞中部分細(xì)胞色素c(cyt c) (15–20%)與心磷脂(CL)緊密結(jié)合。該心磷脂是構(gòu)成線粒體膜的磷脂之一。CL-結(jié)合蛋白具有無活性的三級結(jié)構(gòu)、改變的血紅素袋和破壞的Fe(III)-M80柱向鍵，已知在凋亡過程中起一定作用。這在試圖弄清有關(guān)cyt c–CL相互作用機(jī)理的研究中引起了相當(dāng)?shù)年P(guān)注。在此我們研究了CL與源自馬心和酵母的c-型細(xì)胞色素的結(jié)合反應(yīng)。雖然兩種蛋白具有相似的三級結(jié)構(gòu)，但酵母cyt c穩(wěn)定性低，與馬蛋白相反，它不結(jié)合ATP且沒有促凋亡活性。實(shí)驗(yàn)在有和沒有ATP 和 NaCl的條件下進(jìn)行。這兩種化合物影響（馬 cyt c）-CL的結(jié)合過程進(jìn)而影響該蛋白的促凋亡活性。兩種蛋白具有不同的特性：兩種效應(yīng)劑強(qiáng)烈影響CL與馬cyt c的相互作用，但不影響酵母cyt c。值得注意NaCl 誘導(dǎo)(馬 cyt c)–CL復(fù)合物解離但不影響對應(yīng)的酵母cyt c。從兩種蛋白觀察到的差異強(qiáng)調(diào)特定的結(jié)構(gòu)因素，諸如參與同 CL 或 ATP相互作用的局部結(jié)構(gòu)形態(tài)差異，會明顯地影響cyt c在與脂質(zhì)體反應(yīng)中的特性并進(jìn)而影響該蛋白的促凋亡活性。

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2樓2015-06-24 02:14:25