Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast.

Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast.
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鉴定参与针对叶绿体的前体的蛋白水解加工的两种结构相关的蛋白质。

DOI:
10.1002/j.1460-2075.1992.tb05540.x
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发表时间:
1992
期刊:
The EMBO journal
影响因子:
--
通讯作者:
Lamppa,GK
Lamppa,GK
中科院分区:
--
文献类型:
--
作者:
Oblong,JE;Lamppa,GK

文献摘要

被引文献

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在豌豆中鉴定出两种 145 kDa 和 143 kDa 的蛋白质,它们与叶绿体加工活性共同纯化,该活性裂解主要捕光叶绿素结合蛋白 (preLHCP) 的前体。针对 145/143 kDa 双联体产生的抗血清仅识别叶绿体可溶性提取物中的这两种多肽。在免疫耗竭实验中,抗血清去除了双联体,并且伴随着前LHCP以及Rubisco小亚基和酰基载体蛋白的前体的裂解损失。在所有分级分离过程中,145 和 143 kDa 蛋白质与加工活性峰值并行共洗脱,但未检测到它们作为同二聚体或异二聚体复合物。分别使用145和143 kDa蛋白亲和纯化免疫球蛋白;每种制剂均识别两种多肽,表明它们具有抗原相关性。小麦叶绿体含有大小与 145/143 kDa 双峰相似的可溶性物质。
Two proteins of 145 and 143 kDa were identified in pea which co‐purify with a chloroplast processing activity that cleaves the precursor for the major light‐harvesting chlorophyll binding protein (preLHCP). Antiserum generated against the 145/143 kDa doublet recognizes only these two polypeptides in a chloroplast soluble extract. In immunodepletion experiments the antiserum removed the doublet, and there was a concomitant loss of cleavage of preLHCP as well as of precursors for the small subunit of Rubisco and the acyl carrier protein. The 145 and 143 kDa proteins co‐eluted in parallel with the peak of processing activity during all fractionation procedures, but they were not detectable as a homo‐ or heterodimeric complex. The 145 and 143 kDa proteins were used separately to affinity purify immunoglobulins; each preparation recognized both polypeptides, indicating that they are antigenically related. Wheat chloroplasts contain a soluble species similar in size to the 145/143 kDa doublet.