Characterization of a gene encoding a Ca(2+)-ATPase-like protein in the plastid envelope.
Characterization of a gene encoding a Ca(2+)-ATPase-like protein in the plastid envelope.
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DOI：
10.1073/pnas.90.21.10066
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发表时间：
1993-11
影响因子：
11.1
通讯作者：
Laiqiang Huang;Tom Berkelman;A. Franklin;Neil E. Hoffman
中科院分区：
文献类型：
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作者：
Laiqiang Huang;Tom Berkelman;A. Franklin;Neil E. Hoffman
通过用叶绿体被膜蛋白的抗血清筛选拟南芥表达文库，我们分离到一个具有开放阅读框架的部分cDNA，其编码类似于P型阳离子转运ATP酶的多肽。分离相应的基因组克隆，并对内含子进行鉴定和定位，推导出完整的编码序列。该基因已被命名为PEA 1（质体包膜ATP酶）和预测的多肽PEA 1 p。PEA 1 p具有946个氨基酸，分子量为104 kDa。这种蛋白质与各种哺乳动物质膜Ca（2+）-ATP酶有40-44%的同一性，但缺乏哺乳动物多肽中存在的C-末端钙调蛋白结合结构域。当与哺乳动物质膜Ca（2+）-ATP酶比对时，PEA 1 p具有70至80个氨基酸的N-末端区域，其延伸超出这些酶的N末端。该延伸与质体包膜磷酸转运蛋白的转运肽有一些相似性，并可能起将蛋白质靶向质体的作用。针对PEA 1 p的一部分产生的抗体识别叶绿体内被膜制剂中的单个90- 95-kDa多肽。通过RNA酶保护测定的转录本丰度在根中比在叶中高7- 9倍。质体包膜钙泵的可能作用的建议。
By screening an Arabidopsis expression library with an antiserum against chloroplast envelope proteins, we have isolated a partial cDNA with an open reading frame that encodes a polypeptide similar to P-type cation-transporting ATPases. The corresponding genomic clone was isolated and the complete coding sequence was deduced after identification and mapping of introns. The gene has been designated PEA1 (plastid envelope ATPase) and the predicted polypeptide PEA1p. PEA1p has 946 amino acids and a molecular mass of 104 kDa. This protein is 40-44% identical to various mammalian plasma membrane Ca(2+)-ATPases but lacks the C-terminal calmodulin binding domain present in the mammalian polypeptides. When aligned with mammalian plasma membrane Ca(2+)-ATPases, PEA1p has a 70- to 80-amino acid N-terminal region that extends beyond the N terminus of these enzymes. This extension has some similarity to the transit peptide of the plastid envelope phosphate translocator and may function to target the protein to the plastid. Antibodies raised against a portion of PEA1p recognize a single 90- to 95-kDa polypeptide in chloroplast inner envelope preparations. Transcript abundance as determined by RNase protection was found to be 7- to 9-fold higher in roots than in leaves. Possible roles for a plastid envelope calcium pump are suggested.