Evidence map›Paper›PMID 16997984›Full record

ArticleApplied and environmental microbiology2006

Functional analysis of the twin-arginine translocation pathway in Corynebacterium glutamicum ATCC 13869.

Yoshimi Kikuchi, Masayo Date, Hiroshi Itaya, Kazuhiko Matsui, Long-Fei Wu

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 46 citations in OpenAlex.

  1. Secretory Expression ofJournal of microbiology and biotechnology · 2025
    Article
  2. Transcriptional Regulation of the Creatine Utilization Genes ofFrontiers in bioengineering and biotechnology · 2022
    Article
  3. Proteomes · 2021
    Article
  4. Article
  5. Metabolic engineering ofSynthetic and systems biotechnology · 2019
    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

5 authors at 2 institutions in 2 countries.

Yoshimi KikuchiInstitute of Life Sciences, Ajinomoto Co., Inc., 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki 210-8681, Japan. yoshimi_kikuchi@ajinomoto.com
Masayo Date
Hiroshi Itaya
Kazuhiko Matsui
Long-Fei Wu
Ajinomoto (Japan) · JPInstitut de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Compared to those of other gram-positive bacteria, the genetic structure of the Corynebacterium glutamicum Tat system is unique in that it contains the tatE gene in addition to tatA, tatB, and tatC. The tatE homologue has been detected only in the genomes of gram-negative enterobacteria. To assess the function of the C. glutamicum Tat pathway, we cloned the tatA, tatB, tatC, and tatE genes from C. glutamicum ATCC 13869 and constructed mutants carrying deletions of each tat gene or of both the tatA and tatE genes. Using green fluorescent protein (GFP) fused with the twin-arginine signal peptide of the Escherichia coli TorA protein, we demonstrated that the minimal functional Tat system required TatA and TatC. TatA and TatE provide overlapping function. Unlike the TatB proteins from gram-negative bacteria, C. glutamicum TatB was dispensable for Tat function, although it was required for maximal efficiency of secretion. The signal peptide sequence of the isomaltodextranase (IMD) of Arthrobacter globiformis contains a twin-arginine motif. We showed that both IMD and GFP fused with the signal peptide of IMD were secreted via the C. glutamicum Tat pathway. These observations indicate that IMD is a bona fide Tat substrate and imply great potential of the C. glutamicum Tat system for industrial production of heterologous folded proteins.

Indexed as

Amino Acid SequenceArthrobacterBacterial ProteinsCorynebacterium glutamicumDextranaseEscherichia coli ProteinsGene DeletionGreen Fluorescent ProteinsIndustrial MicrobiologyMembrane Transport ProteinsMolecular Sequence DataPolysaccharidesProtein FoldingSequence Analysis, DNABacterial ProteinsDextranaseEscherichia coli ProteinsGreen Fluorescent ProteinsmaltodextrinMembrane Transport ProteinsPolysaccharidestwin-arginine translocase complex, E coli

Identifiers

PMID16997984
PMCPMC1636197
OpenAlexW2142994017

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.