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KMID : 1234420120400030274
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Korean Journal of Microbiololgy and Biotechnology
2012 Volume.40 No. 3 p.274 ~ p.277
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Cloning, Expression, and Polymerization Assay of FtsZ Protein from Staphylococcus aureus
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Son Sang-Hyeon
Lee Dong-Yun
Kim Ye-Jun
Ko Soo-Ho
Cho Seong-Jun
Jung Hyo-Cheol
Lee Hyung-Ho
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Abstract
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Cytokinesis is the final stage of cell division, dividing one mother cell into two daughter cells. For the cutting of a plasma membrane during bacterial cytokinesis, a tubulin homolog FtsZ protein is recruited from the cytoplasm to the division site. FtsZ protein polymerizes in a GTP-dependent manner and its N-terminal domain has a GTPase activity. In this study, we have begun to characterize FtsZ from Staphylococcus aureus (SA). Full-length SA FtsZ was cloned into pRSFDuet-1 vector and the clone was transformed into a BL21 (DE3) star cell. The recombinant SA FtsZ protein was purified using Ni- NTA affinity chromatography and dialysis. Using a spectrofluorometer, we showed that SA FtsZ undergoes a GTP-dependant polymerization in vitro. The polymer of the SA FtsZ protein disappeared after a few minutes, suggesting that the polymer is degraded as the GTP is consumed. This assay system may well be applied for inhibitor screening targeting S. aureus FtsZ.
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KEYWORD
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Cloning, Expression, and Polymerization Assay of FtsZ Protein from Staphylococcus aureus
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