Abstract
The secretion-responsive regulation of Escherichia coli secA occurs by coupling its translation to the translation and secretion of an upstream regulator, secM (formerly geneX). We revise the translational start site for secM, defining a new signal peptide sequence with an extended amino-terminal region. Mutational studies indicate that certain atypical amino acyl residues within this extended region are critical for proper secA regulation.
| Original language | English |
|---|---|
| Pages (from-to) | 5592-5595 |
| Number of pages | 4 |
| Journal | Journal of Bacteriology |
| Volume | 182 |
| Issue number | 19 |
| DOIs | |
| State | Published - Jan 1 2000 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Immunology
Cite this
Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression. / Sarker, S.; Rudd, K. E.; Oliver, D.
In: Journal of Bacteriology, Vol. 182, No. 19, 01.01.2000, p. 5592-5595.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression
AU - Sarker, S.
AU - Rudd, K. E.
AU - Oliver, D.
PY - 2000/1/1
Y1 - 2000/1/1
N2 - The secretion-responsive regulation of Escherichia coli secA occurs by coupling its translation to the translation and secretion of an upstream regulator, secM (formerly geneX). We revise the translational start site for secM, defining a new signal peptide sequence with an extended amino-terminal region. Mutational studies indicate that certain atypical amino acyl residues within this extended region are critical for proper secA regulation.
AB - The secretion-responsive regulation of Escherichia coli secA occurs by coupling its translation to the translation and secretion of an upstream regulator, secM (formerly geneX). We revise the translational start site for secM, defining a new signal peptide sequence with an extended amino-terminal region. Mutational studies indicate that certain atypical amino acyl residues within this extended region are critical for proper secA regulation.
UR - http://www.scopus.com/inward/record.url?scp=0033801865&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033801865&partnerID=8YFLogxK
U2 - 10.1128/JB.182.19.5592-5595.2000
DO - 10.1128/JB.182.19.5592-5595.2000
M3 - Article
C2 - 10986266
AN - SCOPUS:0033801865
VL - 182
SP - 5592
EP - 5595
JO - Journal of Bacteriology
JF - Journal of Bacteriology
SN - 0021-9193
IS - 19
ER -