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Zhu Y Nam J Humara JM Mysore KS Lee LY Cao H Valentine L Li J Kaiser AD Kopecky AL Hwang HH Bhattacharjee S Rao PK Tzfira T Rajagopal J Yi H Veena Yadav BS Crane YM Lin K Larcher Y Gelvin MJ Knue M Ramos C Zhao X Davis SJ Kim SI Ranjith-Kumar CT Choi YJ Hallan VK Chattopadhyay S Sui X Ziemienowicz A Matthysse AG Citovsky V Hohn B Gelvin SB 《Plant physiology》2003,132(2):494-505
Limited knowledge currently exists regarding the roles of plant genes and proteins in the Agrobacterium tumefaciens-mediated transformation process. To understand the host contribution to transformation, we carried out root-based transformation assays to identify Arabidopsis mutants that are resistant to Agrobacterium transformation (rat mutants). To date, we have identified 126 rat mutants by screening libraries of T-DNA insertion mutants and by using various “reverse genetic” approaches. These mutants disrupt expression of genes of numerous categories, including chromatin structural and remodeling genes, and genes encoding proteins implicated in nuclear targeting, cell wall structure and metabolism, cytoskeleton structure and function, and signal transduction. Here, we present an update on the identification and characterization of these rat mutants. 相似文献
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Duong Van Hop Amos Gaikwad Badam Singh Yadav Malireddy Kodandarami Reddy Sudhir Sopory Sunil Kumar Mukherjee 《The Plant journal : for cell and molecular biology》1999,19(2):153-162
Proliferating cell nuclear antigen (PCNA), a highly conserved DNA polymerase accessory protein of eukary- otic kingdom, has not been studied thoroughly in bio- chemical terms in plants. We describe the isolation of the cDNA encoding PCNA from the pea cDNA library using the PCR approach. The cDNA was used for expression of pea PCNA in bacteria as a fusion protein (GST.PCNA) with the GST tag at the amino terminal end. The GST.PCNA stimulated the partially purified pea DNA polymerases approximately 30-fold. The stimulation was due to the oligomeric form of GST.PCNA. The pea PCNA interacted with the recombinant type I pea topoiso- merase as well as the native pea nuclear topoisomerase I and repressed the DNA relaxation activities. However, the DNA binding activity of Topo I remained undisturbed in the presence of high amounts of PCNA, thereby signify- ing that the catalysis of Topo I was probably affected by PCNA. 相似文献
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