Proteolysis and modulation of the activity of the cell division inhibitor SulA in Escherichia coli lon mutants.
AUTOR(ES)
Canceill, D
RESUMO
Intracellular accumulation of the inducible cell division inhibitor SulA is modulated by proteases that ensure its degradation, namely, the Lon protease and another ATP-dependent protease(s). Lon- cells are UV sensitive because SulA is stable. We asked whether these ATP-dependent proteases are more active when lon cells are grown at high temperature or in synthetic medium since these conditions decrease the UV sensitivity of lon cells. We found that these growth conditions have no direct effect on Lon-independent degradation of SulA. They may, instead, decrease the SulA-FtsZ interaction.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=210862Documentos Relacionados
- Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12.
- Regulation of cell division in Escherichia coli: SOS induction and cellular location of the sulA protein, a key to lon-associated filamentation and death.
- The ATP-Dependent HslVU/ClpQY Protease Participates in Turnover of Cell Division Inhibitor SulA in Escherichia coli
- Protein degradation in Escherichia coli: the lon gene controls the stability of sulA protein.
- An Arabidopsis Homolog of the Bacterial Cell Division Inhibitor SulA Is Involved in Plastid DivisionW⃞
