Evidence map›Paper›PMID 17084862›Full record

ArticleJournal of molecular biology2007

Selective photoaffinity labeling identifies the signal peptide binding domain on SecA.

Monika Musial-Siwek, Sharyn L Rusch, Debra A Kendall

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012
    Review
  14. The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  15. Article
  16. Article
  17. Article
  18. SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011
    Review
  19. Energetics of SecA dimerization.Journal of molecular biology · 2011
    Article
  20. 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

3 authors at 1 institution in 1 country.

Monika Musial-SiwekDepartment of Molecular and Cell Biology, 91 North Eagleville Road, University of Connecticut, Storrs, CT 06269-3125, USA.
Sharyn L Rusch
Debra A Kendall
University of Connecticut · US

Funding

REDESIGN OF STRUCTURAL REGIONS OF ALKALINE PHOSPHATASER01GM037639 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI KENDALL, DEBRA A · 1987 to 2011
$3.8M
NIGMS NIH HHS GM 37639NIGMS NIH HHS R01 GM037639
6 · The paper itself

Abstract

SecA, an ATPase crucial to the Sec-dependent translocation machinery in Escherichia coli, recognizes and directly binds the N-terminal signal peptide of an exported preprotein. This interaction plays a central role in the targeting and transport of preproteins via the SecYEG channel. Here we identify the signal peptide binding groove (SPBG) on SecA addressing a key issue regarding the SecA-preprotein interaction. We employ a synthetic signal peptide containing the photoreactive benzoylphenylalanine to efficiently and specifically label SecA containing a unique Factor Xa site. Comparison of the photolabeled fragment from the subsequent proteolysis of several SecAs, which vary only in the location of the Factor Xa site, reveals one 53 residue segment in common with the entire series. The covalently modified SecA segment produced is the same in aqueous solution and in lipid vesicles. This spans amino acid residues 269 to 322 of the E. coli protein, which is distinct from a previously proposed signal peptide binding site, and contributes to a hydrophobic peptide binding groove evident in molecular models of SecA.

Indexed as

Protein Sorting SignalsAdenosine TriphosphatasesAlkaline PhosphataseAmino Acid SequenceBacterial ProteinsBinding SitesBiotinEscherichia coliFactor XaLipid MetabolismMembrane Transport ProteinsMolecular Sequence DataMutant ProteinsPhenylalaninePhotoaffinity LabelsProtein BindingAdenosine TriphosphatasesAlkaline PhosphataseBacterial ProteinsbenzoylphenylalanineBiotinFactor XaMembrane Transport ProteinsMutant ProteinsPhenylalaninePhotoaffinity LabelsProtein PrecursorsProtein Sorting SignalsSecA ProteinsSEC Translocation Channels

Identifiers

PMID17084862
PMCPMC1851904
OpenAlexW2074516950

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.