Evidence map›Paper›PMID 11741850›Full record

ArticleJournal of bacteriology2002

Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway.

Hongping Tian, Jon Beckwith

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  7. Rational design of a fusion partner for membrane protein expression in E. coli.Protein science : a publication of the Protein Society · 2009
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  14. Target-directed proteolysis at the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  15. Article
  16. Translation arrest of SecM is essential for the basal and regulated expression of SecA.Proceedings of the National Academy of Sciences of the United States of America · 2004
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  17. Article
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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

2 authors at 1 institution in 1 country.

Hongping TianDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
Jon Beckwith
Harvard University · US

Funding

MEMBRANE PROTEINS INVOLVED IN CELL DIVISION IN E.COLIR01GM038922 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BECKWITH, JONATHAN · 1987 to 2005
$2.1M
INSERTION AND TOPOLOGY OF MEMBRANE PROTEINSR37GM038922 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BECKWITH, JONATHAN R · 1987 to 1996
–
NIGMS NIH HHS GM38922NIGMS NIH HHS R01 GM038922
6 · The paper itself

Abstract

We describe the further utilization of a genetic screen that identifies mutations defective in the assembly of proteins into the Escherichia coli cytoplasmic membrane. The screen yielded mutations in each of the known genes encoding components of the E. coli signal recognition particle pathway: ffh, ffs, and ftsY, which encode Ffh, 4.5S RNA, and FtsY, respectively. In addition, the screen yielded mutations in secM, which is involved in regulating levels of the SecA component of the bacterium's protein export pathway. We used a sensitive assay involving biotinylation to show that all of the mutations caused defects in the membrane insertions of three topologically distinct membrane proteins, AcrB, MalF, and FtsQ. Among the mutations that resulted in membrane protein insertion defects, only the secM mutations also showed defects in the translocation of proteins into the E. coli periplasm. Genetic evidence suggests that the S382T alteration of Ffh affects the interaction between Ffh and 4.5S RNA.

Indexed as

ATP-Binding Cassette TransportersMonosaccharide Transport ProteinsAdenosine TriphosphatasesATP-Binding Cassette, Sub-Family C ProteinsBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsEscherichia coliEscherichia coli ProteinsGenes, BacterialMaltose-Binding ProteinsMembrane ProteinsMembrane Transport ProteinsMutationPeriplasmProtein Transport4.5S RNAAcrB protein, E coliAdenosine TriphosphatasesATP-Binding Cassette, Sub-Family C ProteinsATP-Binding Cassette TransportersBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsEscherichia coli ProteinsFfh protein, E coliFtsQ protein, E coliFtsY protein, BacteriaMaltose-Binding Proteinsmaltose transport system, E coliMembrane ProteinsMembrane Transport ProteinsMonosaccharide Transport ProteinsReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsRNA, BacterialRNA, RibosomalSecA ProteinsSEC Translocation ChannelsSignal Recognition Particle

Identifiers

PMID11741850
PMCPMC134764
OpenAlexW1984827214

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.