Evidence map›Paper›PMID 9520394›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

In vitro disassembly and reassembly of an ABC transporter, the histidine permease.

P Q Liu, G F Ames

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Structural basis for substrate specificity of an amino acid ABC transporter.Proceedings of the National Academy of Sciences of the United States of America · 2015
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  13. Side chain and backbone contributions of Phe508 to CFTR folding.Nature structural & molecular biology · 2005
    Article
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  15. Article
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

2 authors at 2 institutions in 1 country.

P Q LiuDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
G F Ames
Harvard University · USUniversity of California, Berkeley · US

Funding

MEMBRANES AND ACTIVE TRANSPORT OF AMINO ACIDSR37DK012121 · NIDDK · UNIVERSITY OF CALIFORNIA BERKELEY · PI AMES, GIOVANNA F · 1986 to 2001
$981k
MEMBRANES AND ACTIVE TRANSPORT OF AMINO ACIDSR01DK012121 · NIDDK · UNIVERSITY OF CALIFORNIA BERKELEY · PI AMES, GIOVANNA F · 1994 to 2004
$720k
NIDDK NIH HHS DK12121NIDDK NIH HHS R01 DK012121NIDDK NIH HHS R37 DK012121
6 · The paper itself

Abstract

The membrane-bound complex of the Salmonella typhimurium periplasmic histidine permease, a member of the ABC transporters (or traffic ATPases) superfamily, is composed of two integral membrane proteins, HisQ and HisM, and two copies of an ATP-binding subunit, HisP. The complex hydrolyzes ATP upon induction of the activity by the liganded soluble receptor, the periplasmic histidine-binding protein, HisJ. Here we take advantage of the modular organization of this system to show that the nucleotide-binding component can be stripped off the integral membrane components, HisQ and HisM. The complex can be reconstituted by using the HisP-depleted membranes containing HisQ and HisM and pure soluble HisP. We show that HisP has high affinity for the HisP-depleted complex, HisQM, and that two HisP molecules are recruited independently of each other for each HisQM unit. The in vitro reassembled complex has entirely normal properties, responding to HisJ and ATPase inhibitors with the same characteristics as the original complex and in contrast to those of soluble HisP. These results show that HisP is absolutely required for ATP hydrolysis, that HisQM cannot hydrolyze ATP, that HisP depends on HisQM to relay the inducing signal from the soluble receptor, HisJ, and that HisQM regulates the ATPase activity of HisP. We also show that HisP changes conformation upon exposure to phospholipids.

Indexed as

Amino Acid Transport Systems, BasicBacterial ProteinsProtein ConformationATP-Binding Cassette TransportersBiological Transport, ActiveDimerizationEscherichia coliMembrane Transport ProteinsPhospholipidsAmino Acid Transport Systems, BasicATP-Binding Cassette TransportersBacterial Proteinshistidine permease, BacteriaMembrane Transport ProteinsPhospholipids

Identifiers

PMID9520394
PMCPMC19864
OpenAlexW2055005326

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.