The primary leaf catalase gene from Nicotiana tabacum and Nicotiana sylvestris.
The primary leaf catalase gene from Nicotiana tabacum and Nicotiana sylvestris.
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来自烟草和樟子松的初级叶过氧化氢酶基因。
DOI：
10.1104/pp.106.1.399
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发表时间：
1994
期刊：
影响因子：
7.4
通讯作者：
Nelson,T
中科院分区：
文献类型：
--
作者：
Schultes,NP;Zelitch,I;McGonigle,B;Nelson,T
C3植物在光合作用的光呼吸途径期间通过乙醇酸氧化酶反应（Zelitch，1992）和过氧化氢酶（EC 1.11. 1.6)在过氧化氢的分解中起作用。主要的烟草叶片过氧化氢酶CAT-1在发芽后15 d左右达到最高水平，并且还存在具有增强的过氧化物活性的次要同工酶CAT-3（Havir和McHale，1987）。已经鉴定出烟草突变体具有比野生型更多的过氧化氢酶蛋白和约40%的增加的过氧化氢酶活性（Zelitch等人，1991年）。当光呼吸快速时，突变体增加了净光合作用（Zelitch，1992）。对过氧化氢酶的作用的另外的兴趣来自于最近关于其在植物防御机制中针对广泛的病原体的功能的报道（Chen等人，1993）和玉米幼苗对低温诱导胁迫的抗性（Prassad等，为了使我们能够产生具有升高和降低的叶片过氧化氢酶水平的转基因植物，我们已经分离并表征了来自烟草（Nicotiana tabacum）（2n= 48）的全长cDNA克隆（1.9kb）和来自欧洲烟草（Nicotiana sylvestris）（2n= 24）的部分cDNA（1.4kb），欧洲烟草是烟草的祖先二倍体之一。tabacum（表I）。了N.樟子松克隆（383个残基）从5 ′编码端缺少约0.4kb（Zelitch等，1991年）。克隆了N. tabacum（492个残基）在5 '端有28个非翻译碱基，随后是开放阅读框中的1476个碱基。该全长N. tabacum过氧化氢酶的预测序列进行了比较。tabacum（489个残基）（Chen等人，1993），N. sylvestris（部分cDNA）（本报告），拟南芥叶（492个残基）（Chevalier等人，1992）、棉籽（492残留）（Ni等人，1990）和玉米幼苗CAT-2（529个残基）（Redinbaugh等人，1988年）。A11植物过氧化氢酶在53和150 bp之间的区域具有高度同源性和近乎完美的同源性。值得注意的是，位置65和79处的His残基是保守的。这是血红素结合位点的区域，类似于牛肝过氧化氢酶中的His 74（Reid等人，1981年）。我们的N。tabacum过氧化氢酶克隆不同于
Large amounts of hydrogen peroxide are generated in C3 plants by the glycolate oxidase reaction during the photorespiratory pathway of photosynthesis (Zelitch, 1992), and catalase (EC 1.11. 1.6) in peroxisomes of leaves functions in the decomposition of hydrogen peroxide. The major tobacco leaf catalase, CAT-1, reaches a maximum leve1 about 15 d postgermination, and a minor isozyme, CAT-3, with enhanced peroxidatic activity is also present (Havir and McHale, 1987). A tobacco mutant has been identified with more catalase protein than wild type and an increased catalase activity of about 40%(Zelitch et al., 1991). The mutant has increased net photosynthesis when photorespiration is rapid (Zelitch, 1992). Additional interest in the role of catalase arises from recent reports of its function in a plant defense mechanism against a broad range of pathogens (Chen et al., 1993) and in resistance to chilling-induced stress in maize seedlings (Prassad et al., 1994).To enable us to produce transgenic plants with elevated and depressed levels of leaf catalase, we have isolated and characterized a full-length cDNA clone (1.9 kb) from Nicotiana tabacum (2n= 48) and a partial cDNA (1.4 kb) from Nicotiana sylvestris (2n= 24), one of the ancestral diploids of N. tabacum (Table I). The N. sylvestris clone (383 residues) lacks about 0.4 kb from the 5’coding end (Zelitch et al., 1991). The full-length leaf catalase cDNA from N. tabacum (492 residues) has 28 untranslated bases at the 5’end followed by 1476 bases in the open reading frame. The predicted amino acid sequence of this full-length N. tabacum catalase was compared to the predicted sequences of catalases from N. tabacum (489 residues)(Chen et al., 1993), N. sylvestris (partial cDNA)(this report), Arabidopsis leaf (492 residues)(Chevalier et al., 1992), cottonseed (492 residues)(Ni et al., 1990), and maize seedling CAT-2 (529 residues)(Redinbaugh et al., 1988). A11 plant catalases have a high degree of homology and near-perfect homology in the region between 53 and 150 bp. Notably the His residues at positions 65 and 79 are conserved. This is the region of the heme-binding site, analogous to His74 in beef liver catalase (Reid et al., 1981). Our N. tabacum catalase clone differs from