MCE domain proteins: conserved inner membrane lipid-binding proteins required for outer membrane homeostasis

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@article{c1b171833c4447d6a2653aae5121c615,
title = "MCE domain proteins:: conserved inner membrane lipid-binding proteins required for outer membrane homeostasis",
abstract = "Bacterial proteins with MCE domains were first described as being important for Mammalian Cell Entry. More recent evidence suggests they are components of lipid ABC transporters. In Escherichia coli, the single-domain protein MlaD is known to be part of an inner membrane transporter that is important for maintenance of outer membrane lipid asymmetry. Here we describe two multi MCE domain-containing proteins in Escherichia coli, PqiB and YebT, the latter of which is an orthologue of MAM-7 that was previously reported to be an outer membrane protein. We show that all three MCE domain-containing proteins localise to the inner membrane. Bioinformatic analyses revealed that MCE domains are widely distributed across bacterial phyla but multi MCE domain-containing proteins evolved in Proteobacteria from single-domain proteins. Mutants defective in mlaD, pqiAB and yebST were shown to have distinct but partially overlapping phenotypes, but the primary functions of PqiB and YebT differ from MlaD. Complementing our previous findings that all three proteins bind phospholipids, results presented here indicate that multi-domain proteins evolved in Proteobacteria for specific functions in maintaining cell envelope homeostasis.",
keywords = "Journal Article, bacteriology , functional clustering , prokaryote",
author = "Isom, {Georgia L.} and Davies, {Nathaniel J.} and Zhi-Soon Chong and Bryant, {Jack A.} and Mohammed Jamshad and Maria Sharif and Cunningham, {Adam F.} and Knowles, {Timothy J.} and Shu-Sin Chng and Cole, {Jeffrey A.} and Henderson, {Ian R.}",
year = "2017",
month = "8",
day = "17",
doi = "10.1038/s41598-017-09111-6",
language = "English",
volume = "7",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - MCE domain proteins:

T2 - conserved inner membrane lipid-binding proteins required for outer membrane homeostasis

AU - Isom, Georgia L.

AU - Davies, Nathaniel J.

AU - Chong, Zhi-Soon

AU - Bryant, Jack A.

AU - Jamshad, Mohammed

AU - Sharif, Maria

AU - Cunningham, Adam F.

AU - Knowles, Timothy J.

AU - Chng, Shu-Sin

AU - Cole, Jeffrey A.

AU - Henderson, Ian R.

PY - 2017/8/17

Y1 - 2017/8/17

N2 - Bacterial proteins with MCE domains were first described as being important for Mammalian Cell Entry. More recent evidence suggests they are components of lipid ABC transporters. In Escherichia coli, the single-domain protein MlaD is known to be part of an inner membrane transporter that is important for maintenance of outer membrane lipid asymmetry. Here we describe two multi MCE domain-containing proteins in Escherichia coli, PqiB and YebT, the latter of which is an orthologue of MAM-7 that was previously reported to be an outer membrane protein. We show that all three MCE domain-containing proteins localise to the inner membrane. Bioinformatic analyses revealed that MCE domains are widely distributed across bacterial phyla but multi MCE domain-containing proteins evolved in Proteobacteria from single-domain proteins. Mutants defective in mlaD, pqiAB and yebST were shown to have distinct but partially overlapping phenotypes, but the primary functions of PqiB and YebT differ from MlaD. Complementing our previous findings that all three proteins bind phospholipids, results presented here indicate that multi-domain proteins evolved in Proteobacteria for specific functions in maintaining cell envelope homeostasis.

AB - Bacterial proteins with MCE domains were first described as being important for Mammalian Cell Entry. More recent evidence suggests they are components of lipid ABC transporters. In Escherichia coli, the single-domain protein MlaD is known to be part of an inner membrane transporter that is important for maintenance of outer membrane lipid asymmetry. Here we describe two multi MCE domain-containing proteins in Escherichia coli, PqiB and YebT, the latter of which is an orthologue of MAM-7 that was previously reported to be an outer membrane protein. We show that all three MCE domain-containing proteins localise to the inner membrane. Bioinformatic analyses revealed that MCE domains are widely distributed across bacterial phyla but multi MCE domain-containing proteins evolved in Proteobacteria from single-domain proteins. Mutants defective in mlaD, pqiAB and yebST were shown to have distinct but partially overlapping phenotypes, but the primary functions of PqiB and YebT differ from MlaD. Complementing our previous findings that all three proteins bind phospholipids, results presented here indicate that multi-domain proteins evolved in Proteobacteria for specific functions in maintaining cell envelope homeostasis.

KW - Journal Article

KW - bacteriology

KW - functional clustering

KW - prokaryote

U2 - 10.1038/s41598-017-09111-6

DO - 10.1038/s41598-017-09111-6

M3 - Article

C2 - 28819315

VL - 7

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 8608

ER -