Title : Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon.

Pub. Date : 1997 Apr 28

PMID : 9180687






4 Functional Relationships(s)
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1 Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon. sula putative ATP-dependent Lon protease Escherichia coli
2 When LacZ protein was fused at its C-terminus to 8 or 20 amin acid residues from the C-terminal region of SulA the protein was stable in lon+ cells. sula putative ATP-dependent Lon protease Escherichia coli
3 These results indicate that the C-terminal 20 residues of SulA permit recognition by, and complex formation with, Lon, and are necessary, but not sufficient, for degradation by Lon. sula putative ATP-dependent Lon protease Escherichia coli
4 These results indicate that the C-terminal 20 residues of SulA permit recognition by, and complex formation with, Lon, and are necessary, but not sufficient, for degradation by Lon. sula putative ATP-dependent Lon protease Escherichia coli