Xu P, Harvey A J, Fincher G B
Department of Plant Science, University of Adelaide, South Australia.
FEBS Lett. 1994 Jul 11;348(2):206-10. doi: 10.1016/0014-5793(94)00610-5.
Two cDNAs have been isolated from libraries generated from poly(A)+RNA of young barley roots and leaves, using a cDNA encoding barley (1-->3)-beta-glucanase isoenzyme GII as a probe. Nucleotide sequence analyses and ribonuclease protection assays show that the two cDNAs differ only in the length of their 3'-untranslated regions; the corresponding mRNAs are likely to originate from a single gene by tissue-specific processing at separate polyadenylation sites. When the coding region of the cDNA is expressed in E. coli, the resultant protein catalyses the hydrolysis of (1-->3)-beta-glucan with an action pattern characteristic of a (1-->3)-beta-glucan endohydrolase (EC 3.2.1.39). The enzyme has been designated isoenzyme GV of the barley (1-->3)-beta-glucanase family).
以编码大麦(1→3)-β-葡聚糖酶同工酶GII的cDNA为探针,从大麦幼根和叶片的poly(A)+RNA构建的文库中分离出两个cDNA。核苷酸序列分析和核糖核酸酶保护试验表明,这两个cDNA仅在其3'-非翻译区的长度上有所不同;相应的mRNA可能通过在不同聚腺苷酸化位点的组织特异性加工,源自单个基因。当cDNA的编码区在大肠杆菌中表达时,产生的蛋白质催化(1→3)-β-葡聚糖的水解,其作用模式具有(1→3)-β-葡聚糖内切酶(EC 3.2.1.39)的特征。该酶被命名为大麦(1→3)-β-葡聚糖酶家族的同工酶GV。