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	1. Cloning, expression analysis, and detection method of the S12-RNase gene existing in three pear species (Pyrus bretschneideri, P. pyrifolia, and P. ussuriensis)
	Zhang Lin,Liu Min,Tan Xiaofeng,Song Zhibo,Long Hongxu,Cao Yufen,Li Xiugen
	Forestry 23 November 2012
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	Abstract:A specific forward primer was designed based on the principle of highest similarity, and employed in 3' RACE using Chinese white pear (Pyrus bretschneideri) cultivar 'Yingzhiqing' as materials. The full length cDNA of PbS12-RNase was successfully amplified and deposited in GenBank (Accession No. EU081889). At the amino acid level, the PbS12-RNase exhibited the highest similarity (97.3%) with MdSf-RNase of Malus domestica, and only six amino acid differences were present in the two S-RNases. Phylogenetic analysis of rocaceous S-RNases indicated that the PbS12-RNase clustered with maloideous S-RNases, forming a subfamily-specific not species-specific group. Some intraspecific genetic distance of the S-RNases, in addition, was greater than interspecific genetic distance. In 'Yingzhiqing', the PbS12-allele was specifically expressed in style. Moreover, the expression level of this gene was extremely low at the small bud stage, and subsequently increased rapidly at the bid bud stage and bell stage. A method for rapid detection of the PbS12-allele was developed via PbS12-allele-specefic primers design based on multiple sequence comparisons. Application of the PbS12-allele-specefic primers in 59 cultivars from four pear species showed that the PbS12-allele not only existed in P. bretschneideri, but in P. pyrifolia and P. ussuriensis as well. The present study could provide a scientific base for fully clarifying the mechanism of pear GSI at the molecular level.
	TO cite this article:Zhang Lin,Liu Min,Tan Xiaofeng, et al. Cloning, expression analysis, and detection method of the S12-RNase gene existing in three pear species (Pyrus bretschneideri, P. pyrifolia, and P. ussuriensis)[OL].[23 November 2012] http://en.paper.edu.cn/en_releasepaper/content/4497964


	2. Molecular cloning and sequence characterization of the full-length cDNA encoding S28-RNase from Xinjiang pear (Pyrus sinkiangenis)
	Liu Min,Zhang Lin,Wang Mingmei,Tan Xiaofeng,Song Zhibo,Li Xiugen,Cao Yufen
	Forestry 31 October 2012
	Show/Hide Abstract \| Cite this paper︱Full-text: PDF (0 B)

	Abstract: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.
	TO cite this article:Liu Min,Zhang Lin,Wang Mingmei, et al. Molecular cloning and sequence characterization of the full-length cDNA encoding S28-RNase from Xinjiang pear (Pyrus sinkiangenis)[OL].[31 October 2012] http://en.paper.edu.cn/en_releasepaper/content/4493661

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