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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2
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The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2

机译：玉蜀黍BAM7基因编码的一种蛋白质类似的结构和催化性能拟南芥BAM2

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摘要

Starch accumulates in the plastids of green plant tissues during the day to provide carbon for metabolism at night. Starch hydrolysis is catalyzed by members of the beta-amylase (BAM) family, which in Arabidopsis thaliana (At) includes nine structurally and functionally diverse members. One of these enzymes, AtBAM2, is a plastid-localized enzyme that is unique among characterized beta-amylases since it is tetrameric and exhibits sigmoidal kinetics. Sequence alignments show that the BAM domains of AtBAM7, a catalytically inactive, nuclear-localized transcription factor with an N-terminal DNA-binding domain, and AtBAM2 are more closely related to each other than they are to any other AtBAM. Since the BAM2 gene is found in more ancient lineages, it was hypothesized that the BAM7 gene evolved from BAM2. However, analysis of the genomes of 48 flowering plants revealed 12 species that appear to possess a BAM7 gene but lack a BAM2 gene. Upon closer inspection, these BAM7 proteins have a greater percent identity to AtBAM2 than to AtBAM7, and they share all of the AtBAM2 functional residues that BAM7 proteins normally lack. It is hypothesized that these genes may encode BAM2-like proteins although they are currently annotated as BAM7-like genes. To test this hypothesis, a cDNA for the short form of corn BAM7 (ZmBAM7-S) was designed for expression in Escherichia coli. Small-angle X-ray scattering data indicate that ZmBAM7-S has a tetrameric solution structure that is more similar to that of AtBAM2 than to that of AtBAM1. In addition, partially purified ZmBAM7-S is catalytically active and exhibits sigmoidal kinetics. Together, these data suggest that some BAM7 genes may encode a functional BAM2. Exploring and understanding the beta-amylase gene structure could have an impact on the current annotation of genes.
机译：淀粉积累在绿色植物的叶绿体组织在白天提供碳晚上的新陈代谢。催化的beta-amylase (BAM)家庭,在拟南芥(在)包括9个结构上和功能上多样化的成员。plastid-localized酶中是独一无二的beta-amylases因为它是特点四聚物的s形动力学和展品。序列比对表明的BAM域AtBAM7、催化地活动与一个nuclear-localized转录因子氨基端dna结合域,AtBAM2比他们更彼此密切相关任何其他AtBAM。在更古老的血统,这是假设从BAM2 BAM7基因进化。48开花植物的基因组分析显示12个物种似乎拥有BAM7但缺乏BAM2基因的基因。检查,这些BAM7蛋白有一个更大的身份AtBAM2比AtBAM7百分比他们分享的所有AtBAM2功能残留通常,BAM7蛋白质缺乏。假设这些基因可能编码虽然他们目前BAM2-like蛋白质标注为BAM7-like基因。假设,cDNA短形式的玉米BAM7 (ZmBAM7-S)是为表达设计的大肠杆菌。数据显示,ZmBAM7-S四聚物的解决方案结构更类似AtBAM2比AtBAM1。部分纯化ZmBAM7-S催化地活动和展览s形动力学。这些数据表明,一些BAM7基因可能编码功能BAM2。理解beta-amylase基因结构可能会影响当前的注释基因。

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