Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons
Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons
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DOI：
10.1093/pcp/pce108
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发表时间：
2001-08-01
影响因子：
4.9
通讯作者：
Nishimura, M
中科院分区：
文献类型：
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作者：
Fukao, Y;Hayashi, Y;Nishimura, M
为了阐明过氧化物酶体膜蛋白（pmp），我们对其中一个主要的pmp蛋白PMP38进行了表征。拟南芥cDNA的氨基酸序列包含331个氨基酸，与人类PMP34和假丝酵母PMP47线粒体ATP/ADP载体蛋白同源物具有较高的相似性。我们预计PMP38定位于过氧化物酶体膜上，因为它具有过氧化物酶体膜靶向信号。南瓜子叶的细胞分离和免疫细胞化学分析表明，PMP38作为一个完整的膜蛋白定位在过氧化物酶体膜上。南瓜子叶中PMP38的含量在黑暗处理6 d后增加，达到最高蛋白水平，随后下降。幼苗光照导致蛋白质含量显著降低。这些结果清楚地表明，在glyoxysomal转化为叶片过氧化物酶体的过程中，glyoxysomal膜蛋白PMP38发生了巨大的变化，其他glyoxysomal酶，特别是脂肪酸β -氧化循环的酶，定位于glyoxysomal基质中。
In order to clarify the peroxisomal membrane proteins (PMPs), we characterized one of the major PMPs, PMP38. The deduced amino acid sequence for its cDNA in Arabidopsis thaliana contained polypeptides with 331 amino acids and had high similarity with those of Homo sapiens PMP34 and Candida boidinii PMP47 known as homologues of mitochondrial ATP/ADP carrier protein. We expected PMP38 to be localized on peroxisomal membranes, because it had the membrane peroxisomal targeting signal. Cell fractionation and immunocytochemical analysis using pumpkin cotyledons revealed that PMP38 is localized on peroxisomal membranes as an integral membrane protein. The amount of PMP38 in pumpkin cotyledons increased and reached the maximum protein level after 6 d in the dark but decreased thereafter. Illumination of the seedlings caused a significant decrease in the amount of the protein. These results clearly showed that the membrane protein PMP38 in glyoxysomes changes dramatically during the transformation of glyoxysomes to leaf peroxisomes, as do the other glyoxysomal enzymes, especially enzymes of the fatty acid beta -oxidation cycle, that are localized in the matrix of glyoxysomes.