Kleczkowski L A, Sokolov L N, Luo C, Villand P
Department of Plant Physiology, Umeå University, Sweden.
Z Naturforsch C J Biosci. 1999 May-Jun;54(5-6):353-8. doi: 10.1515/znc-1999-5-610.
A cDNA, ApL1a, corresponding to a homologue of the large subunit of ADP-glucose pyrophosphorylase (AGPase), has been isolated/characterised by screening a cDNA library prepared from leaves of Arabidopsis thaliana, followed by rapid amplification of cDNA 3'-ends (3'-RACE). Within the 1685 nucleotide-long sequence (excluding polyA tail), an open reading frame encodes a protein of 522 amino acids (aa), with a calculated molecular weight of 57.7 kDa. The derived aa sequence does not contain any discernible transit peptide cleavage site motif, similarly to two other recently sequenced full-length Arabidopsis homologues for AGPase, and shows ca. 58-78% identity to homologous proteins from other plants/tissues. The corresponding gene was found to be expressed in all tissues examined (rosette and stem leaves, stems, flowers and fruits). The ubiquitous expression of the gene is consistent with its critical role in starch synthesis in Arabidopsis.
通过筛选从拟南芥叶片制备的cDNA文库，随后进行cDNA 3'末端的快速扩增（3'-RACE），已分离并鉴定出一个与ADP-葡萄糖焦磷酸化酶（AGPase）大亚基同源的cDNA，即ApL1a。在1685个核苷酸长的序列（不包括聚腺苷酸尾）中，一个开放阅读框编码一个522个氨基酸（aa）的蛋白质，计算分子量为57.7 kDa。与最近测序的另外两个拟南芥AGPase全长同源物类似，推导的氨基酸序列不包含任何可识别的转运肽切割位点基序，并且与来自其他植物/组织的同源蛋白显示约58-78%的同一性。发现相应的基因在所有检测的组织（莲座叶和茎生叶、茎、花和果实）中表达。该基因的普遍表达与其在拟南芥淀粉合成中的关键作用一致。
