http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Staphylococcus aureus FtsZ의 클로닝, 발현 및 폴리머 형성 활성 분석
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 ) 한국미생물생명공학회(구 한국산업미생물학회) 2012 한국미생물·생명공학회지 Vol.40 No.3
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.