Staphylococcus aureus FtsZ의 클로닝, 발현 및 폴리머 형성 활성 분석
분야
자연과학 > 생물
저자
손상현 ( Sang Hyeon Son ) , 이동윤 ( Dong Yun Lee ) , 김예준 ( Ye Jun Kim ) , 고수호 ( Soo Ho Ko ) , 조성준 ( Seong Jun Cho ) , 정효철 ( Hyo Cheol Jung ) , 이형호 ( Hyung Ho Lee )
발행기관
한국미생물생명공학회(구 한국산업미생물학회)
간행물정보
한국미생물·생명공학회지 2012년, 제40권 제3호, 274~277페이지(총4페이지)
파일형식
05212045.pdf [무료 PDF 뷰어 다운로드]
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    영문초록
    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 aGTP-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 aGTP-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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