TABLE 2.
Effects of replacement of the signal anchor sequence of PulC
Plasmida | Protein | Sequenceb | Complementation of ΔpulC
|
|
---|---|---|---|---|
Noninduced | Induced | |||
pCHAP1305 | PulC | LAQLTWEFFKIIL | 80 | 100 |
pCHAP1232 | MalE-′PulC | IEGRISEFFKIIL | 0 | 0 |
pCHAP1292 | MalESP-′PulC | A*AKIDLEFFKIIL | 30 | 80 |
pCHAP1315 | MalESA-′PulC | DAKIDLEFFKIIL | 50 | 80 |
pCHAP1316 | PhoESP-′PulC | ASVQA*AEFFKIIL | 80 | 100 |
pCHAP1298 | PulASPCD-′PulC | G*CDNSAEFFKIIL | 30 | 100 |
pCHAP1299 | PulASPCS-′PulC | G*CSNSAEFFKIIL | 0 | 0 |
All are derivatives of pSU18 (2), with the gene fusion under lacZp control (induced with 1 mM IPTG).
Sequences indicated are at the junction between the sections of the protein near the beginning of the periplasmic domain of PulC. Residues in italics are derived from MalE, PhoE, or PulA and linker-encoded residues; other amino acids are from PulC. The last residue of the PulC sequence indicated is position 50. The sequence of unmutated PulC upstream of this position is LAQLTWKIIL. ∗, signal peptidase cleavage site.