Molecular characterization of Escherichia coli FtsE and FtsX.

E.P.H. de Leeuw; B. Graham; G.J. Philips; C.M. ten Hagen-Jongman ten; B. Oudega; S. Luirink

doi:10.1046/j.1365-2958.1999.01245.x

Molecular characterization of Escherichia coli FtsE and FtsX.

E.P.H. de Leeuw, B. Graham, G.J. Philips, C.M. ten Hagen-Jongman ten, B. Oudega, S. Luirink

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

The genes ftsE and ftsX are organized in one operon together with ftsY. FtsY codes for the receptor of the signal recognition particle (SRP) that functions in targeting a subset of inner membrane proteins. We have found no indications for a structural relationship between FtsE/X and FtsY. Evidence is presented that FtsE and FtsX form a complex in the inner membrane that bears the characteristics of an ATP-binding cassette (ABC)-type transporter. FtsE is a hydrophilic nucleotide-binding protein that has a tendency to dimerize and associates with the inner membrane through an interaction with the integral membrane protein FtsX. An FtsE null mutant showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport.

Original language	English
Pages (from-to)	983-993
Number of pages	11
Journal	Molecular Microbiology
Volume	31
DOIs	https://doi.org/10.1046/j.1365-2958.1999.01245.x
Publication status	Published - 1999

Access to Document

10.1046/j.1365-2958.1999.01245.x

Persistent URL (handle)

Persistent link

Cite this

@article{b7d0ec0c2cc7495dbe2dcc65b9c327df,

title = "Molecular characterization of Escherichia coli FtsE and FtsX.",

abstract = "The genes ftsE and ftsX are organized in one operon together with ftsY. FtsY codes for the receptor of the signal recognition particle (SRP) that functions in targeting a subset of inner membrane proteins. We have found no indications for a structural relationship between FtsE/X and FtsY. Evidence is presented that FtsE and FtsX form a complex in the inner membrane that bears the characteristics of an ATP-binding cassette (ABC)-type transporter. FtsE is a hydrophilic nucleotide-binding protein that has a tendency to dimerize and associates with the inner membrane through an interaction with the integral membrane protein FtsX. An FtsE null mutant showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport.",

author = "{de Leeuw}, E.P.H. and B. Graham and G.J. Philips and {ten Hagen-Jongman ten}, C.M. and B. Oudega and S. Luirink",

year = "1999",

doi = "10.1046/j.1365-2958.1999.01245.x",

language = "English",

volume = "31",

pages = "983--993",

journal = "Molecular Microbiology",

issn = "0950-382X",

publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Molecular characterization of Escherichia coli FtsE and FtsX.

AU - de Leeuw, E.P.H.

AU - Graham, B.

AU - Philips, G.J.

AU - ten Hagen-Jongman ten, C.M.

AU - Oudega, B.

AU - Luirink, S.

PY - 1999

Y1 - 1999

N2 - The genes ftsE and ftsX are organized in one operon together with ftsY. FtsY codes for the receptor of the signal recognition particle (SRP) that functions in targeting a subset of inner membrane proteins. We have found no indications for a structural relationship between FtsE/X and FtsY. Evidence is presented that FtsE and FtsX form a complex in the inner membrane that bears the characteristics of an ATP-binding cassette (ABC)-type transporter. FtsE is a hydrophilic nucleotide-binding protein that has a tendency to dimerize and associates with the inner membrane through an interaction with the integral membrane protein FtsX. An FtsE null mutant showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport.

AB - The genes ftsE and ftsX are organized in one operon together with ftsY. FtsY codes for the receptor of the signal recognition particle (SRP) that functions in targeting a subset of inner membrane proteins. We have found no indications for a structural relationship between FtsE/X and FtsY. Evidence is presented that FtsE and FtsX form a complex in the inner membrane that bears the characteristics of an ATP-binding cassette (ABC)-type transporter. FtsE is a hydrophilic nucleotide-binding protein that has a tendency to dimerize and associates with the inner membrane through an interaction with the integral membrane protein FtsX. An FtsE null mutant showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport.

U2 - 10.1046/j.1365-2958.1999.01245.x

DO - 10.1046/j.1365-2958.1999.01245.x

M3 - Article

SN - 0950-382X

VL - 31

SP - 983

EP - 993

JO - Molecular Microbiology

JF - Molecular Microbiology

ER -

Molecular characterization of Escherichia coli FtsE and FtsX.

Abstract

Access to Document

Persistent URL (handle)

Fingerprint

Cite this