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Functional Analysis Of Two ARF GTPase Activating Proteins Of Magnaporthe Oryzae In The Growth And Pathogenic Process

Posted on:2016-12-11Degree:MasterType:Thesis
Country:ChinaCandidate:X LiuFull Text:PDF
GTID:2323330512472760Subject:Plant pathology
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Rice blast is an important fungal diseases on rice production in the world,annual losses of up to hundreds of millions of hectares of rice,seriously affecting global food security.Therefore,it’s important to study the Magnaporthe oryzae and the disease epidemic.Rice blast was caused by M.oryzae,the current approach to combat rice blast is mainly taking breeding for disease resistance,but due to the nature of the pathogen populations in diverse and volatile,constantly the new breeding resistant varieties often can not resist a new type of M.oryzae pathogenic infection,or loss of use value in a few years after plant.At present,although there are ways to identify the alteration of the pathogenicity,but to prevent rice blast fundamentally,we have to do research on the aspects of growth and development of M.oryzae and pathogenic molecular mechanism.In recent years,with the publication of M.oryzae genome sequence and the matures of genetic transformation technique,the steps of the research on the aspects of growth and development of M.oryzae and pathogenic molecular mechanism have speed up,and also provides a theoretical and technical support for the new target to the rice blast.Intracellular transport of substances is essential for the survival and growth of cells,which can promote the formation of cell membranes,lysosomes,and make cells secrete proteins,hormones and neurotransmitters and uptake by endocytosis of exogenous molecules.Endocytosis is a complex transport process that can commonly found in yeast and mammalian plasma membrane,which includes take-up of a variety of proteins and lipid kinases,phosphoric acid(lipid)enzymes,signaling molecules and the actin cytoskeleton arrangement.In this process,plasma membrane proteins,lipids and some macromolecules are allocated by intracellular vesicle transport to the early endosomes,followed by degradation in the vacuole or mature endosome,or as a protein receptors are reused through the cycle.Vesicle transport controlled by a variety of regulatory factors,ADP ribosylation factor(ARF)is one of them,and they are included in the Ras superfamily.Meanwhile,ARF is also involved in the regulating the activity of phospholipase D,and play a more significant role in material transport and signal transduction process in the cell.Generally,ARF is activated by a guanine nucleotide exchange(GEF),converts the inactive GDP-bound form into the active GTP-bound form through GDP/GTP replacement.The activated GTPase then associates with proteins such as SNAREs and cargo,which are targeted for transport to the next compartment along the vesicular transport pathway.This complex are stabilized by another effector of the GTPase,the GTPase-activating protein(GAP).When threshold amount of such complexes is achieved,the associated deformation of the membrane filter,vesicle formation is initiated,and finally ARF will be back to the cytoplasm.Thus,GAPs play an important role in vesicular transport.The object of this study are MoGlo3,MoGcs1,they are a class of GAPs.We analysed the function of MoGlo3,MoGcs1 in the growth and pathogenic molecular mechanism of M.oryzae.The deletion mutant △Moglo3 showed slower vegetative and invasive hyphal growth,and fewer lesion on the leaves of rice,barley,but AMogcsl showed no defect in vegetative and lesion on the leaves of rice,barley compared with the wild type strain Guy11.The deletion mutant △AMoglo3 can not produce condia and become more sensitive to external stress.AMogcsl produced lower amount of condia and increased the rate of appressorium compared to the wide type strain Guyl 1.All the results show that,MoGlo3 is involved in the regulation of the development and the pathogenicity of M.oryzae.Since SNARE proteins were found,it has been to dominate a bubble fusion center component.We have a positioning analysis of a SNARE protein MoSyn8 in Magnaporthe oryza,we found that the mutant can not form a Actin ring.
Keywords/Search Tags:Magnaporthe oryzae, GAPs, MoGlo3, MoGcs1, MoSyn8, Pathogenicity
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