Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease.

doi:10.1016/j.jmb.2007.06.083

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Article

Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease.

Journal of molecular biology - 14 Sept 2007

Führer Frank, Müller Alexandra, Baumann Holger, Langklotz Sina, Kutscher Blanka, Narberhaus Franz

Abstract excerpt

The membrane-anchored FtsH protease is essential in Escherichia coli as it adjusts the cellular amount of LpxC, the key enzyme in lipopolysaccharide (LPS) biosynthesis. Both accumulation and depletion of LpxC are toxic to E. coli. By continuous proteolysis of LpxC, FtsH maintains a low concentration of LpxC and, hence, the proper equilibrium between LPS and phospholipids. The C terminus of LpxC is required for...

Topics

ATP-Dependent Proteases
Amidohydrolases
Amino Acid Sequence
Amino Acid Substitution
Enzyme Stability
Escherichia coli
Escherichia coli Proteins
Glutathione Transferase
Membrane Proteins
Molecular Sequence Data
Mutation
Protein Processing, Post-Translational
Solubility

Source

Open in PubMed

Identifiers

PMID: 17651755
DOI: 10.1016/j.jmb.2007.06.083

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