Study On The Function Of Carya Cathayensis SVP Gene

The SVP gene is a key inhibitor in flower development.Its main function has been proven,but the specific function in different species remain to be studied.In order to reveal the evolutionary history and pattern of SVP gene;to explore the effects of Carya cathayensis SVP gene(CcSVP)in plant morphology and flowering time;to identification of flower development-related genes and specific domains that interact with CcSVP protein.This study uesd bioinformatics to analyze the evolutionary history of SVP gene and its selection pressure during evolution;heterologous transformation of Arabidopsis thaliana by Agrobacterium infection to explore the function of CcSVP gene;yeast two-hybrid system used to explore the interaction of CcSVP with other genes.The main results are as follows:1.Phylogenetic analysis indicated that the SVP genes were under purifying selection pressure during the evolution.The development of SVP genes towards a more conservative direction,it means that the function and structure of SVP genes had stabilized.The branch sites of these selection pressures are distributed in MADS-box and K-box,and their changes are one of the important reasons for the differentiation of SVP gene with AGL24 and JOINTLESS;2.Transgenic studies showed that overexpression of CcSVP in Arabidopsis thaliana caused delayed and prolonged flowering,loss of petals,stamen shortening,scarring of lateral branches,and shortening of fruit pods.These indicated that CcSVP has an important influence on the morphogenesis,flowering,flower type and fruit development of the plant.3.The full-length protein interaction experiments showed that CcSVP could interact with CcAP1 and CcSOC1,and the interaction intensity between CcSVP and CcAP1 was stronger than that of CcSVP and CcSOC1;CcSVP did not interact with CcFLC;4.Partial fragment protein interaction experiments showed that the single domain of CcSVP and CcAP1 could not complete the interaction with the full-length protein alone,and it was necessary for multiple domains or even full-length proteins to exert their ability to interact.