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

Abstract:

: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, ATPgammaS, 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Seong IS,Oh JY,Yoo SJ,Seol JH,Chung CH

doi

10.1016/s0014-5793(99)00935-7

keywords:

subject

Has Abstract

pub_date

1999-07-30 00:00:00

pages

211-4

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)00935-7

journal_volume

456

pub_type

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