Abstract
The Escherichia coli TolC acts as a channel-tunnel in the transport of molecules across the outer membrane. We previously showed that the region extending from the 50th to the 60th amino acid residues from the carboxy terminus is involved in the transport activity of TolC. To clarify which amino acids are important to the activity, we mutated the gene coding these residues and examined the activity of the mutant TolCs. The results showed that leucine at position 412, the 60th amino acid residue from the carboxy terminal end, is important. Further mutational research on the residue suggested that TolC required a nonpolar amino acid residue at position 412 to express its activity.
| Original language | English |
|---|---|
| Pages (from-to) | 81-89 |
| Number of pages | 9 |
| Journal | Microbial Pathogenesis |
| Volume | 33 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2002 |
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Keywords
- Antibiotics
- E. coli
- Heat-stable enterotoxin
- Outer membrane
- Secretion
- TolC
ASJC Scopus subject areas
- Microbiology
- Infectious Diseases
Cite this
Site-directed mutagenesis studies of the amino acid residue at position 412 of Escherichia coli TolC which is required for the activity. / Yamanaka, Hiroyasu; Nomura, Tomohiko; Morisada, Naoyuki; Shinoda, Sumio; Okamoto, Keinosuke.
In: Microbial Pathogenesis, Vol. 33, No. 2, 2002, p. 81-89.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Site-directed mutagenesis studies of the amino acid residue at position 412 of Escherichia coli TolC which is required for the activity
AU - Yamanaka, Hiroyasu
AU - Nomura, Tomohiko
AU - Morisada, Naoyuki
AU - Shinoda, Sumio
AU - Okamoto, Keinosuke
PY - 2002
Y1 - 2002
N2 - The Escherichia coli TolC acts as a channel-tunnel in the transport of molecules across the outer membrane. We previously showed that the region extending from the 50th to the 60th amino acid residues from the carboxy terminus is involved in the transport activity of TolC. To clarify which amino acids are important to the activity, we mutated the gene coding these residues and examined the activity of the mutant TolCs. The results showed that leucine at position 412, the 60th amino acid residue from the carboxy terminal end, is important. Further mutational research on the residue suggested that TolC required a nonpolar amino acid residue at position 412 to express its activity.
AB - The Escherichia coli TolC acts as a channel-tunnel in the transport of molecules across the outer membrane. We previously showed that the region extending from the 50th to the 60th amino acid residues from the carboxy terminus is involved in the transport activity of TolC. To clarify which amino acids are important to the activity, we mutated the gene coding these residues and examined the activity of the mutant TolCs. The results showed that leucine at position 412, the 60th amino acid residue from the carboxy terminal end, is important. Further mutational research on the residue suggested that TolC required a nonpolar amino acid residue at position 412 to express its activity.
KW - Antibiotics
KW - E. coli
KW - Heat-stable enterotoxin
KW - Outer membrane
KW - Secretion
KW - TolC
UR - http://www.scopus.com/inward/record.url?scp=0036385660&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036385660&partnerID=8YFLogxK
U2 - 10.1006/mpat.2002.0519
DO - 10.1006/mpat.2002.0519
M3 - Article
C2 - 12202107
AN - SCOPUS:0036385660
VL - 33
SP - 81
EP - 89
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
SN - 0882-4010
IS - 2
ER -