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

被引:60
作者
Seong, IS
Oh, JY
Yoo, SJ
Seol, JH
Chung, CH [1 ]
机构
[1] Seoul Natl Univ, Coll Nat Sci, Dept Mol Biol, Seoul 151742, South Korea
[2] Seoul Natl Univ, Coll Nat Sci, Res Ctr Cell Differentiat, Seoul 151742, South Korea
关键词
ATP-dependent protease; ATPase; HslVU; protease La; SulA; cell division;
D O I
10.1016/S0014-5793(99)00935-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 nonhydrolyzable analog, ATP gamma S, 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, (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:211 / 214
页数:4
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