| Summary: | 碩士 === 中山醫學院 === 生物化學研究所 === 85 === XpsG,H,I and J,having homologous leader sequence of type
IV pilin,arecytoplasmic membrane proteins that require for the
secretion of extracellularproteins in Xanthomonas campestris pv.
campestris. The objective of this researchis to study the
protein-protein interaction between XpsG,H,I and J and the
putativepilin-like structure. The specific aims include the
construction of expression vector,the overexpression of
recombinant proteins,the induction of antibody and
investigationof the protein-protein interaction in XC1701. In
this study,four expression vectors wereconstructed. Among them,
the recombinant protein of XpsG and XpsI were expressed and
purifiedby both pET32a and pQE9 expression vectors from E.coli
BL21(DE3) and M15[pREP4] strain. Theantibodies against XpsG and
XpsI were also obtained by immunizing rabbits with purified
recombinantproteins. Gel filtration chromatography and Western
blot analysis were then performed to analyze thecofraction of
XpsD,XpsG and XpsI proteins. The preliminary data showed that
XpsG and XpsI,which wereeluted in the same fraction,were not
cofractionation with XpsD. The protein-protein interaction
betweenXpsG and XpsI in XC1701 still need other experiment such
as immunoaffinity chromatography analysis to bedirect evidence
for perfomed.
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