Article
Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides.
The Journal of biological chemistry - 16 Mar 2007
Tullman-Ercek Danielle, DeLisa Matthew P, Kawarasaki Yasuaki, Iranpour Pooya, Ribnicky Brian, Palmer Tracy, Georgiou George
Abstract excerpt
The Escherichia coli genome encodes at least 29 putative signal peptides containing a twin arginine motif characteristic of proteins exported via the twin arginine translocation (Tat) pathway. Fusions of the putative Tat signal peptides plus six to eight amino acids of the mature proteins to three reporter proteins (short-lived green fluorescent protein, maltose-binding protein (MBP), and alkaline phosphatase)...
Topics
- Amino Acid Sequence
- Biological Transport
- Computational Biology
- Escherichia coli
- Escherichia coli Proteins
- Genome, Bacterial
- Green Fluorescent Proteins
- Membrane Transport Proteins
- Molecular Sequence Data
- Mutation
- Plasmids
- Protein Folding
- Protein Sorting Signals