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ATP‐dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli
Author(s) -
Seong Ihn Sik,
Oh Ji Yeon,
Yoo Soon Ji,
Seol Jae Hong,
Chung Chin Ha
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00935-7
Subject(s) - escherichia coli , maltose binding protein , cell division , biochemistry , mutant , protease , biology , atpase , atp hydrolysis , enzyme , ftsz , fusion protein , microbiology and biotechnology , cell , recombinant dna , gene
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.