mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N

Claire Punginelli; Bérengère Ize; Nicola R. Stanley; Valley Stewart; Gary Sawers; Ben C. Berks; Tracy Palmer

doi:10.1128/JB.186.18.6311-6315.2004

mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N

Claire Punginelli
, Bérengère Ize
, Nicola R. Stanley
, Valley Stewart
, Gary Sawers
, Ben C. Berks
, Tracy Palmer

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (alphabetagamma)3 configuration. The FdnG subunit carries a Tat-dependent signal peptide, which localizes the protein complex to the periplasmic side of the membrane. We noted that substitution of the first arginine (R5) in the twin arginine signal sequence of FdnG for a variety of other amino acids resulted in a dramatic (up to 60-fold) increase in the levels of protein synthesized. Bioinformatic analysis suggested that the mRNA specifying the first 17 codons of fdnG forms a stable stem-loop structure. A detailed mutational analysis has demonstrated the importance of this mRNA stem-loop in modulating FDH-N translation.

Original language	English
Pages (from-to)	6311-6315
Number of pages	5
Journal	Journal of Bacteriology
Volume	186
Issue number	18
DOIs	https://doi.org/10.1128/JB.186.18.6311-6315.2004
Publication status	Published - 2004

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10.1128/JB.186.18.6311-6315.2004

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title = "mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N",

abstract = "Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (alphabetagamma)3 configuration. The FdnG subunit carries a Tat-dependent signal peptide, which localizes the protein complex to the periplasmic side of the membrane. We noted that substitution of the first arginine (R5) in the twin arginine signal sequence of FdnG for a variety of other amino acids resulted in a dramatic (up to 60-fold) increase in the levels of protein synthesized. Bioinformatic analysis suggested that the mRNA specifying the first 17 codons of fdnG forms a stable stem-loop structure. A detailed mutational analysis has demonstrated the importance of this mRNA stem-loop in modulating FDH-N translation.",

author = "Claire Punginelli and B{\'e}reng{\`e}re Ize and Stanley, \{Nicola R.\} and Valley Stewart and Gary Sawers and Berks, \{Ben C.\} and Tracy Palmer",

year = "2004",

doi = "10.1128/JB.186.18.6311-6315.2004",

language = "English",

volume = "186",

pages = "6311--6315",

journal = "Journal of Bacteriology",

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publisher = "American Society for Microbiology",

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TY - JOUR

T1 - mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N

AU - Punginelli, Claire

AU - Ize, Bérengère

AU - Stanley, Nicola R.

AU - Stewart, Valley

AU - Sawers, Gary

AU - Berks, Ben C.

AU - Palmer, Tracy

PY - 2004

Y1 - 2004

N2 - Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (alphabetagamma)3 configuration. The FdnG subunit carries a Tat-dependent signal peptide, which localizes the protein complex to the periplasmic side of the membrane. We noted that substitution of the first arginine (R5) in the twin arginine signal sequence of FdnG for a variety of other amino acids resulted in a dramatic (up to 60-fold) increase in the levels of protein synthesized. Bioinformatic analysis suggested that the mRNA specifying the first 17 codons of fdnG forms a stable stem-loop structure. A detailed mutational analysis has demonstrated the importance of this mRNA stem-loop in modulating FDH-N translation.

AB - Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (alphabetagamma)3 configuration. The FdnG subunit carries a Tat-dependent signal peptide, which localizes the protein complex to the periplasmic side of the membrane. We noted that substitution of the first arginine (R5) in the twin arginine signal sequence of FdnG for a variety of other amino acids resulted in a dramatic (up to 60-fold) increase in the levels of protein synthesized. Bioinformatic analysis suggested that the mRNA specifying the first 17 codons of fdnG forms a stable stem-loop structure. A detailed mutational analysis has demonstrated the importance of this mRNA stem-loop in modulating FDH-N translation.

U2 - 10.1128/JB.186.18.6311-6315.2004

DO - 10.1128/JB.186.18.6311-6315.2004

M3 - Article

C2 - 15342602

SN - 0021-9193

VL - 186

SP - 6311

EP - 6315

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 18

ER -

mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N

Abstract

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