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Modification of PATase by L/F-transferase generates a ClpS-dependent N-end rule substrate in Escherichia coli.
- Source :
-
The EMBO journal [EMBO J] 2009 Jun 17; Vol. 28 (12), pp. 1732-44. Date of Electronic Publication: 2009 May 14. - Publication Year :
- 2009
-
Abstract
- The N-end rule pathway is conserved from bacteria to man and determines the half-life of a protein based on its N-terminal amino acid. In Escherichia coli, model substrates bearing an N-degron are recognised by ClpS and degraded by ClpAP in an ATP-dependent manner. Here, we report the isolation of 23 ClpS-interacting proteins from E. coli. Our data show that at least one of these interacting proteins--putrescine aminotransferase (PATase)--is post-translationally modified to generate a primary N-degron. Remarkably, the N-terminal modification of PATase is generated by a new specificity of leucyl/phenylalanyl-tRNA-protein transferase (LFTR), in which various combinations of primary destabilising residues (Leu and Phe) are attached to the N-terminal Met. This modification (of PATase), by LFTR, is essential not only for its recognition by ClpS, but also determines the stability of the protein in vivo. Thus, the N-end rule pathway, through the ClpAPS-mediated turnover of PATase may have an important function in putrescine homeostasis. In addition, we have identified a new element within the N-degron, which is required for substrate delivery to ClpA.
- Subjects :
- Amino Acid Motifs
Amino Acid Sequence
Bacterial Outer Membrane Proteins metabolism
Carrier Proteins chemistry
Chromatography, Affinity
Dipeptides metabolism
Endopeptidase Clp chemistry
Endopeptidase Clp metabolism
Escherichia coli Proteins chemistry
Hydrophobic and Hydrophilic Interactions
Ligands
Models, Biological
Molecular Sequence Data
Mutant Proteins metabolism
Protein Binding
Substrate Specificity
Aminoacyltransferases metabolism
Carrier Proteins metabolism
Escherichia coli enzymology
Escherichia coli Proteins metabolism
Metabolic Networks and Pathways
Protein Processing, Post-Translational
Transaminases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1460-2075
- Volume :
- 28
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- The EMBO journal
- Publication Type :
- Academic Journal
- Accession number :
- 19440203
- Full Text :
- https://doi.org/10.1038/emboj.2009.134