[Objective] The aim of this study was to identify the roles of an aquaporin gene GhNIP5.1 in upland cotton （Gossypium hirsutum） by bioinformatics method, so as to provide theoretical basis for further research on aquaporins in upland cotton. [Method] In silico molecular cloning was adopted to obtain an ORF sequence of GhNIP5.1 gene, which was then analyzed by the methods of bioinformatics. The coding region of GhNIP5.1 gene was obtained by analyzing the cotton genome se-quence published in NCBI. [Result] This cDNA sequence had a complete open reading frame of 897 bp and encoded 298 amino acid residues, including the con-served domain NPA （Asn-Pro-Ala） of MIP superfamily. The similarities of GhNIP5.1 deduced amino acid sequences from upland cotton with grape and Arabidopsis, were up to 89.3% and 83.2%, respectively. GhNIP5.1 was most similar in homology and 3-D structure of proteins to AtNIP5.1 among the nine members of NIP family in Arabidopsis. The coding region length of GhNIP5.1 gene was 2 067 bp, and it con-tained three introns and four exons. Al the exon-intron junctions of the gene con-tained the consensus splicing site pair GT-AG. [Conclusion] GhNIP5.1 gene probably has similar physiological functions with Arabidopsis AtNIP5.1.
Artemisinin, a sesquiterpene lactone endoperoxide derived from Artemisia annua L, forms the basis of the most important medicines for treating malaria in use today. In the study, a total of 41 full genes coded cytochrome P450 monooxygenases were identified from NCBI. These genes were classified into 11 families in 3 gene clans according to sequence similarity. One of the first interesting features in sequence alignment was that the CYP82, CYP83 and CYP716 families specific in Arabidopsis genome were present in Artemisia, and the CYP92 specific in rice was also present in Artemisia. The physical and chemical properties and structure characteristics of the identified P450s were studied. The results showed their secondary structures were very similar and their senior structures mainly contained α-helix.
