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Molecular cloning and sequence characterization of the full-length cDNA encoding S28-RNase from Xinjiang pear (Pyrus sinkiangenis)
Liu Min 1,Zhang Lin 2 * #,Wang Mingmei 3,Tan Xiaofeng 2,Song Zhibo 2,Li Xiugen 4,Cao Yufen 5
1.Key Laboratory of Cultivation and Protection for Non-Wood Forest Trees, Ministry of Education, Central South University of Forestry and Technology, ChangSha 410004
2.Key Laboratory of Cultivation and Protection for Non-Wood Forest Trees, Ministry of Education, Central South University of Forestry and Technology, Changsha 410004
3.Colledge of Forestry, Central South University of Forestry and Technology, Changsha 410004
4.Zhengzhou Fruit Research Institute, Chinese Academy of Agricultural Sciences, Zhengzhou 450009, China
5.Research Institute of Pomology, Chinese Academy of Agricultural Sciences, Xingcheng 125100, China
*Correspondence author
#Submitted by
Subject:
Funding: New Teachers‘Foundation for Doctor Stations, Ministry of Education(No.20094321120001), Scientific Research Foundation of Central South University of Forestry & Technology (No.2009004A), Senior Talent Introduction Foundation of Central South University of Forestry & Technology (No.104-0129)
Opened online: 7 November 2012
Accepted by: none
Citation: Liu Min,Zhang Lin,Wang Mingmei.Molecular cloning and sequence characterization of the full-length cDNA encoding S28-RNase from Xinjiang pear (Pyrus sinkiangenis)[OL]. [ 7 November 2012] http://en.paper.edu.cn/en_releasepaper/content/4493661
 
 
The full length cDNA encoding S28-RNase (GenBank accession No. EF566872) was cloned from styles of Xinjiang pear (Pyrus sinkiangeni) cultivar 'Kuerlexiangli' by Reverse transcription-PCR (RT-PCR) and Rapid Amplification of cDNA Ends (RACE) technology. The S28-RNase cDNA contained 865 nucleotides including a complete open reading frame (ORF) predicted to encode a protein of 228 amino acids. The S28-RNase displayed the basic structural features of pear S-RNases, i.e. five conserved regions (C1, C2, C3, RC4 and C5) and a hypervariable (HV) region. At the deduce amino acid level, S28-RNase showed 58.4% to 99.6% similarity with other pear S-RNases. The isoeletric point (pI) and molecular weight (Mw) of S28-RNase were predicted to be 9.30 and 25.6 kDa, respectively. The S28-RNase showed the conserved motifs with two histidine residue, His-61 and His-117 which are essential for T2/S type RNase activity. It also presented eight cysteine residues mostly conserved in S-RNases, forming four disulfide bridges important for the formation or stabilization of their tertiary structure. The S28-RNase also showed seven potential N-glycosilation sites, of which only one, Asn-145, conserved in rosaceous S-RNases, whose glycans may be important in the folding and stabilization of the core structure.
Keywords:Gametophytic self-incompatibility (GSI); 'Kuerlexiangli'; Rapid Amplification of cDNA Ends; S28-RNase gene
 
 
 

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