Evidence map›Paper›PMID 20696931›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Plasticity of lipid-protein interactions in the function and topogenesis of the membrane protein lactose permease from Escherichia coli.

Mikhail Bogdanov, Philip Heacock, Ziqiang Guan, William Dowhan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.7field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 97 citations in OpenAlex.

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  8. Tracking Membrane Protein Dynamics in Real Time.The Journal of membrane biology · 2021
    Review
  9. Review
  10. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Mikhail BogdanovDepartment of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA. mikhail.v.bogdanov@uth.tmc.edu
Philip Heacock
Ziqiang Guan
William Dowhan
Duke Medical Center · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
NIGMS NIH HHS GM-069338NIGMS NIH HHS R37 GM020478NIGMS NIH HHS R37 GM20478NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

Phosphatidylcholine (PC) has been widely used in place of naturally occurring phosphatidylethanolamine (PE) in reconstitution of bacterial membrane proteins. However, PC does not support native structure or function for several reconstituted transport proteins. Lactose permease (LacY) of Escherichia coli, when reconstituted in E. coli phospholipids, exhibits energy-dependent uphill and energy-independent downhill transport function and proper conformation of periplasmic domain P7, which is tightly linked to uphill transport function. LacY expressed in cells lacking PE and containing only anionic phospholipids exhibits only downhill transport and lacks native P7 conformation. Reconstitution of LacY in the presence of E. coli-derived PE, but not dioleoyl-PC, results in uphill transport. We now show that LacY exhibits uphill transport and native conformation of P7 when expressed in a mutant of E. coli in which PC completely replaces PE even though the structure is not completely native. E. coli-derived PC and synthetic PC species containing at least one saturated fatty acid also support the native conformation of P7 dependent on the presence of anionic phospholipids. Our results demonstrate that the different effects of PE and PC species on LacY structure and function cannot be explained by differences in the direct interaction of the lipid head groups with specific amino acid residues alone but are due to more complex effects of the physical and chemical properties of the lipid environment on protein structure. This conclusion is supported by the effect of different lipids on the proper folding of domain P7, which indirectly influences uphill transport function.

Indexed as

Base SequenceDNA PrimersEscherichia coliEscherichia coli ProteinsKineticsLactoseMembrane LipidsModels, MolecularMonosaccharide Transport ProteinsMutant ProteinsPhosphatidylcholinesPhosphatidylethanolaminesPlasmidsProtein Structure, TertiarySymportersDNA PrimersEscherichia coli ProteinsLactoseLacY protein, E coliMembrane LipidsMonosaccharide Transport ProteinsMutant ProteinsPhosphatidylcholinesphosphatidylethanolaminePhosphatidylethanolaminesSymporters

Identifiers

PMID20696931
PMCPMC2930521
OpenAlexW2131895086

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.