ATP‐dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli

FEBS Letters

Chung, Chin Ha¹  Oh, Ji Yeon¹  Seong, Ihn Sik¹  Yoo, Soon Ji¹  Seol, Jae Hong¹ 

[1] Department of Molecular Biology and Research Center for Cell Differentiation, College of Natural Sciences, Seoul National University, Seoul 151-742, South Korea

关键词: ATP-dependent protease;    ATPase;    HslVU;    Protease La;    SulA;    Cell division;   

DOI  :  10.1016/S0014-5793(99)00935-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

HslVU is an ATP-dependent protease consisting of two multimeric components, the HslU ATPase and the HslV peptidase. To gain an insight into the role of HslVU in regulation of cell division, the reconstituted enzyme was incubated with SulA, an inhibitor of cell division in Escherichia coli, or its fusion protein with maltose binding protein (MBP). HslVU degraded both proteins upon incubation with ATP but not with its non-hydrolyzable analog, ATPγS, indicating that the degradation of SulA requires ATP hydrolysis. The pulse-chase experiment using an antibody raised against MBP-SulA revealed that the stability of SulA increased in hsl mutants and further increased in lon/hsl double mutants, indicating that SulA is an in vivo substrate of HslVU as well as of protease La (Lon). These results suggest that HslVU in addition to Lon plays an important role in regulation of cell division through degradation of SulA.

【 授权许可】

Unknown