Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery.
The recently described Tat protein translocation system in Escherichia coli recognizes its protein substrates by the consensus twin arginine (SRRXFLK) motif in the signal peptide. The signal sequence of E. coli pre-pro-penicillin amidase bears two arginine residues separated by one aspargine and does not resemble the Tat-targeting motif but can nevertheless target the precursor to the Tat pathway. Mutational studies have shown that the hydrophobic core region acts in synergism with the positive charged N-terminal part of the signal peptide as a Tat recognition signal and contributes to the efficient Tat targeting of the pre-pro-penicillin amidase.
Ignatova
Zoya
Z
Institut für Biotecnologie II, Technische Universität Hamburg-Harburg, Denickestrasse 15, Hamburg, 21073, Germany. ignatova@tu-harburg.de
Hörnle
Claudia
C
Nurk
Alan
A
Kasche
Volker
V
D020816:Amino Acid Motifs / Q000502:physiology; D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010399:Penicillin Amidase / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology; D021382:Protein Sorting Signals / Q000502:physiology*; D021381:Protein Transport / Q000502:physiology; D013329:Structure-Activity Relationship
D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D021382:Protein Sorting Signals; C408585:twin-arginine translocase complex, E coli; D010399:Penicillin Amidase